A home a world away from home

For Nicholas Maurer, an international PhD student from Australia pursuing his degree in social and engineering systems through the Institute of Data, Systems, and Society, MIT was a lifelong goal. Growing up in Australia with a background in physics and engineering, he worked as a researcher, but never stopped wondering what it would be like to study at MIT. 

When the opportunity came two years ago, he and his wife Andrea made the leap across the world, bringing their young children Elaine, 5, and Zachary, 3, with them. “It was always on my radar,” Maurer recalls. “Coming to MIT felt like a dream come true.”

Weighing their options

Maurer’s wife, Andrea, explains that it was “always in the cards” for the couple to travel for his studies, but neither of them expected this step to come after they had kids. Nevertheless, when Nicholas received multiple PhD offers, the decision came down to one crucial factor: support for their family of four. Together, the couple researched resources before deciding on the move. MIT's commitment to student parents stood out immediately.

As they learned more about the MIT Grant for Graduate Students with Children, on-campus childcare options, and Westgate — MIT's dedicated student family housing — their interest grew. They could tell that MIT cared about building a real home for its families. 

Finding community in Westgate and beyond

Their residence has become far more than housing for the Maurer family; it's the heart of their MIT experience. Maurer credits the dedicated family accommodation with helping them form instant connections. “The biggest support has been Westgate,” he says. 

For both Nicholas and Andrea, the international character of Westgate held special meaning. After moving from Australia, being surrounded by families from around the world eased the transition. The couple eventually became more involved with the Westgate community as parent resource coordinators, helping maintain connections among other parents and spouses.

When the family initially arrived at MIT, Andrea also found friendships through MIT Spouses and Partners Connect (MIT S&PC). “Meeting other spouses provided great comfort as others shared their experiences navigating this new life,” she explained, adding that it was helpful to see how others supported their partners through various MIT programs.

Although financial cuts necessitated S&PC's closure last year, she has been able to keep the spirit of the initiative going through informal meetups and coffee hours.

Parenting at MIT

The family has made the most of MIT's community offerings, attending student-parent lunches during finals week, visiting Rock Spot for rock climbing, and enjoying free ice cream events. They've also taken advantage of MIT Activities Committee discounts for family activities, allowing them to explore the greater Boston area.

Although the supports are substantial, Maurer is candid about the realities of balancing a PhD with parenting. “It's not for the fainthearted,” he says. “It takes a lot of time management and being honest with your capacity. I have learned to say no to some social activities or enrolling in that extra class I’m interested in, in favor of focusing on my core research objectives and supporting my family.”

Amid the challenges, though, there's genuine joy. “It's been amazing seeing our kids meet and play with kids from all over the world,” Maurer reflects. “MIT is an amazing place.”

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Carter Stubbs named Institute auditor

Carter Stubbs has been appointed MIT’s Institute auditor, effective Nov. 2. 

Stubbs, who currently serves as audit assistant director for IT Audit and Advisory Services, has been a member of the MIT community for more than 11 years and brings deep institutional knowledge, highly salient management experience, and a forward-looking vision to the role. Stubbs will succeed Michael Moody, who has served as Institute auditor for 12 years and will retire from MIT in October. 

Executive Vice President and Treasurer Glen Shor announced the news today in a letter to MIT’s Academic Council.

“Carter stood out in a competitive field of candidates thanks to his impressive audit and IT expertise, collaborative leadership style, and robust understanding of MIT’s complex operations,” Shor says. “He has earned the trust and admiration of colleagues inside and outside the division and is well-positioned to write its next chapter.”

As Institute auditor, Stubbs will lead a team of internal auditors responsible for independently evaluating MIT’s academic, research, and administrative processes, including operations at Lincoln Laboratory. He will oversee a comprehensive, risk-based audit and advisory program spanning financial, operational, compliance, and technology reviews across the Institute. 

The MIT Audit Division maintains a dual reporting structure to ensure its independence. Stubbs and the audit team work for the MIT Corporation Risk and Audit Committee, but receive administrative support from the MIT Office of the Executive Vice President and Treasurer.

“Carter’s strong technical command of IT auditing and hands-on experience auditing and advising on major systems implementations will be especially valuable as the Institute continues to advance its business and digital transformation roadmap,” says Pat Callahan, the chair of the Risk and Audit Committee. “The committee will be well-served by his experience with our current audit program, his demonstrated leadership and sound judgment, and his wide-ranging knowledge of the Institute.”

Stubbs joined MIT in 2015 as a senior auditor of information technology, steadily assuming increasing responsibility for information technology, data analytics, and advisory services. He now leads those functions for the Audit Division and serves on the division’s management team. Working closely with the Institute auditor, Stubbs shapes annual risk assessment work, audit planning, and broader division strategy while managing the oversight of complex engagements; contributing to quality assurance and advancing the division’s capabilities; and proactively responding to emerging institutional needs. Stubbs collaborates with leaders from across MIT’s academic, research, administrative, and technology units, including Lincoln Laboratory, and facilitates communications with Institute governance.

During his time at MIT, Stubbs has built an extensive network of partners and developed a multifaceted understanding of the Institute’s operating model, higher education and research risks, and the leadership judgment necessary to navigate complex institutional matters. He has helped steer cross-Institute efforts involving research data management, artificial intelligence, cybersecurity, and digital transformation. A graduate of the 2025 MIT Leader to Leader program, Stubbs served as an advisor to the MIT Working Group on Artificial Intelligence in Administration and Operations and is a member of the MIT Data Incident Response Team. 

“I am honored to serve as MIT’s next Institute auditor,” says Stubbs. “The Audit Division plays an essential role in advancing the Institute’s mission of education and research through independent insight, trusted partnership, and thoughtful perspective on risk. I look forward to building on the division’s strong foundation and helping the Institute navigate an increasingly complex regulatory and risk environment.”

Prior to joining MIT, Stubbs held audit roles at Clean Harbors Environmental Services, Denbury Resources, and PricewaterhouseCoopers, where he developed broad expertise in IT and business process controls across multiple industries. He holds certifications as both a certified internal auditor and certified information systems auditor and earned a BBA in information and operations management from Texas A&M University.

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Batteries that safely break down in the GI tract could improve ingestible devices

Using materials safe for human consumption, MIT researchers have created tiny batteries that could be used to power ingestible electronic devices. Such batteries could make the devices safer for patients and minimize the environmental impact of the batteries after they are excreted.

In a new study, the researchers showed that the batteries, which generate 1.84 volts, could power two different types of devices: an RFID tag that can transmit from the stomach, and a capsule that produces a small electrical current that stimulates production of ghrelin, the hunger hormone.

This type of battery, which contains electrodes made from magnesium and molybdenum trioxide, could also be deployed in other ingestible devices for sensing or therapeutic applications, the researchers say.

“For many of the systems we’re developing, we need power, and we power the system through different ways,” says Giovanni Traverso, a professor of mechanical engineering at MIT, a gastroenterologist at Brigham and Women’s Hospital, and an associate member of the Broad Institute of MIT and Harvard. “Often, we use batteries, so the question here was: Could we develop a battery that was bioresorbable, and then apply that across a range of application areas?”

Traverso is the senior author of the paper, which appears today in Nature Chemical Engineering. Former MIT postdoc Mehmet Girayhan Say is the paper’s lead author.

Biocompatible batteries

Over the past decade, Traverso and his collaborators have developed ingestible capsules that can monitor vital signs, deliver a variety of drugs, and detect opioid overdoses.

Not all of these devices require a power source. For those that do, the researchers have powered the devices from an external source that wirelessly transmits power, harvested power from the GI tract, or used small coin batteries. However, those batteries, which usually contain lithium, silver oxide, or other metals, could pose a safety risk if the battery’s protective coating was damaged while traveling through the GI tract. 

To create a safer battery and allow the systems to be fully self-contained with no external power needed, the researchers turned to metals that can act as electrodes but are safe for human consumption in small amounts — magnesium and molybdenum trioxide. 

“Those materials are known to be relatively safe. That was the biggest driver, thinking about materials that can be tolerated by humans,” Traverso says.

The researchers used magnesium to create the battery’s anode and molybdenum trioxide for the cathode. The battery also contains an ionic liquid gel electrolyte, and the entire system is bioresorbable, meaning that it can be fully broken down and absorbed by the body. The researchers designed two different versions of the battery that could be used for different applications —a disc 7.5 millimeters in diameter and a rectangular bar 24 millimeters long.

To test how the batteries would behave in the GI tract, the researchers first exposed them to a highly acidic solution similar to gastric juice. They found that the batteries function normally for about three days, then their performance begins to slowly decline. Within a few weeks, they break down completely.

The researchers then incorporated the rectangular battery into a degradable device they first reported in 2023, which is designed to deliver a small electrical current to the lining of the stomach. In their earlier work, Traverso’s lab showed that this jolt could stimulate endocrine cells in the stomach to produce ghrelin.

Stimulating ghrelin secretion could prove useful for treating diseases that involve nausea or loss of appetite, such as cachexia (loss of body mass that can occur in patients with cancer or other chronic diseases).

The initial version of that device was powered by two silver oxide coin batteries, similar to those used in FDA-approved ingestible devices. By replacing those with the new magnesium-molybdenum oxide batteries, the researchers made nearly the entire device — with the exception of a printed circuit board — bioresorbable. Any components that aren’t absorbed can be passed through the GI tract and excreted.

In the new study, the researchers showed that new battery was strong enough to generate continuous electrical stimulation for up to three days. Tests in animals showed that 20 minutes of stimulation within the stomach could boost ghrelin levels by about 50 percent.

“What makes this work exciting is that we were able to show that a bioresorbable battery is not just a concept. It can actually power clinically relevant functions inside the gastrointestinal tract and then simply dissolve,” Say says.

Battery-powered communication

The researchers then incorporated the battery into a RFID device, which they designed to help patients adhere to their medication schedules. This capsule can transmit its location from within the GI tract via a bioresorbable RFID tag made from molybdenum and cellulose. 

An earlier RFID system, known as SAFARI and reported by Traverso’s lab in January, used passive RFID tags, powered by harvested energy, which limits the communication range. 

In the new study, tests in animals showed that RFID tags could be effectively powered by a disc-shaped bioresorbable battery. With the new battery, the device could transmit continuously from the GI tract, and with a longer range (up to 1.5 meters).

The researchers are now planning a clinical trial for the SAFARI system, which they expect will begin in about two years. Such systems could not only be safer for patients, but also would reduce the environmental impact of batteries that would eventually be excreted into the sewage system. 

“The benefits are twofold: one, the ability to be bioresorbable, but also the potential to minimize environmental impact because the materials will be degraded in the environment as well,” Traverso says.

The research was funded by Novo Nordisk, the Karl van Tassel Career Development Professorship, MIT’s Department of Mechanical Engineering, the Brigham and Women’s Hospital Division of Gastroenterology, and the U.S. Advanced Research Projects Agency for Health (ARPA-H). 

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Unmasking “zombie cells” in aging tissue with an AI-powered barcode

As we age, some of the cells in our body enter a state of senescence, in which they stop dividing but do not die. Those senescent cells can contribute to age-related disorders such as cancer, tissue degeneration, and inflammatory diseases.

In an advance that could lead to better ways to diagnose and treat those diseases, MIT researchers have developed a noninvasive way to detect biomarkers of senescence. Their method is based on Raman microscopy, which can reveal the biochemical composition of cells without harming them.

By combining Raman microscopy with gene expression data at single-cell resolution from the same cells, the researchers were able to identify unique “barcodes” that can be used to quickly identify senescent cells. This study was done in mouse cells, but the researchers are now working on adapting it for use with human tissue.

“You can imagine that one day we may develop an endoscope that can look inside your body and identify cellular senescence,” says Jeon Woong Kang, an MIT research scientist and one of the senior authors of the study.

The research is part of a National Institutes of Health initiative called the Cellular Senescence Network, which is pursuing a deeper understanding of senescence in hopes of developing therapies that could combat some of the tissue-damaging effects of senescent cells.

Peter So, director of the MIT Laser Biomedical Research Center (LBCR) and an MIT professor of biological engineering and mechanical engineering, and Jian Shu, an assistant professor at Massachusetts General Hospital (MGH) and Harvard Medical School, and an associate member of the Broad Institute and Ragon Institute, are also senior authors of the paper, which appears today in Nature Aging. Lead authors of the paper are Ke Zhang, an instructor at MGH and Harvard Medical School; Xingjian Chen, a postdoc at MGH and Harvard Medical School; Francesco Monticolo, a postdoc at MGH and Harvard Medical School; and Salvatore Sorrentino, a postdoc at MIT. 

Characterizing senescence

Cell senescence is often triggered by DNA damage, which leads to an irreversible arrest of the cell cycle. These cells don’t die, but they undergo significant changes to their shape, metabolic processes, and gene expression profiles. 

The immune system is responsible for clearing out these “zombie cells,” but as people age, this process becomes less efficient. When senescent cells accumulate, they may contribute to sagging skin, muscle weakness, and chronic conditions such as osteoarthritis and type 2 diabetes.

Cellular senescence also has beneficial effects, playing critical roles in embryonic development and tissue regeneration.

“Senescence is not just a pathological condition,” So says. “The idea behind the NIH Cellular Senescence Network is to take a very comprehensive approach to understand senescence and identify senescent cells, because it plays a role in so many normal physiological conditions and many pathological conditions.”

Scientists have already identified a few biomarkers for senescence, including two proteins called p16 and p21, which are involved in halting the cell cycle. However, those proteins can only be identified using a process that ends up destroying the cells.

The MIT team wanted to find a way to noninvasively identify senescent cells using Raman microscopy. Unlike RNA-sequencing, which consumes the cells as it analyzes them, Raman microscopy is a nondestructive technique that reveals the chemical composition of tissues or cells by shining near-infrared or visible light on them.

In the new study, the researchers used Raman microscopy in conjunction with spatial RNA sequencing — a technique that reveals where genes are active within a tissue — to identify new markers of senescence. By combining these two techniques, they were able to generate a much broader picture of the distinctive features of senescent cells, including gene expression levels, spatial location, and other biochemical information.

“Our idea was to look at many different features to characterize senescence. That’s why we wanted to combine both single-cell gene expression and Raman microscopy, so that we can characterize the senescence from two complementary views,” Shu says.

Using both methods of analysis, the researchers examined skin and lung tissue from 2-month-old mice and 26-month-old mice.

One of the most dramatic changes seen in both lung and skin cells was an increase in lipid synthesis in older cells, along with accumulation of lipids. How this affects the physiology of the cells is not yet known, the researchers say.

The researchers also found some effects that were specific to each tissue. In senescent skin cells, they discovered that cellular pathways associated with muscle contraction and with remodeling of collagen and the extracellular matrix were significantly affected. And in aged lung tissue, they found increased activity of genes involved in immune activation and inflammation.

In future work, the researchers hope to study further what role these changes play in senescent cells. 

Identifying senescent cells

Using these data, the researchers were able to identify combinations of Raman peaks that correlate with senescence. These peaks, which represent specific chemical bonds, are linked to the presence of certain lipids, proteins, or other molecules.

“Combining the most important Raman features with the most important gene signatures, we were able to create a barcode that can help us to identify senescent cells in a more unbiased way,” Sorrentino says. “Using this barcode, we can focus on a few Raman bands that emerged as the most informative in this work.” Using these bands, it could be possible to identify senescent cells by looking for just those bands of the Raman spectrum. This could help to enable diagnostics that would detect cells that have become senescent. 

To help make that possible, the researchers are now working on a higher-speed version of their Raman imaging system. Currently, it takes about 30 hours to analyze a tissue sample about one square millimeter in size, but they hope to develop a system that can quickly pick out the Raman barcodes they identified from larger samples.

The research was funded by the National Institutes of Health and Massachusetts General Hospital. 

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A new understanding of how enzymes influence bacterial protein production

Antimicrobial resistance is one of the most pressing global health and development challenges of our time. Bacteria and other pathogens are rapidly developing resistance to existing treatments, making infections harder to treat. Without new approaches, minor inconveniences today, such as routine surgeries or even a paper cut, could become life-threatening tomorrow. 

Now, an international group of scientists reports the discovery of aminovaleramididine synthetase (AvaS), the first identified pyridoxal phosphate (PLP)-dependent enzyme responsible for producing a chemical modification linked to how bacteria respond to metabolic stress. This discovery sheds new light on how bacteria use RNA modification to control protein production, opening new avenues to study bacterial adaptation and identify future targets and better strategies for developing antimicrobial therapeutics. 

The work was led by researchers from the Singapore-MIT Alliance for Research and Technology’s Antimicrobial Resistance interdisciplinary research group (SMART AMR), alongside collaborators from MIT, Nanyang Technological University in Singapore, and institutions in the United States, Poland, and France.

“While many RNA modifications have been known for decades, researchers are still uncovering the full extent of their roles. The discovery of AvaS opens a previously unknown chapter in RNA biology and is an important step forward in our understanding of processes relevant to antimicrobial resistance,” says Professor Peter Dedon, co-lead principal investigator at SMART AMR, professor of biological engineering at MIT, and co-corresponding author of a new paper on the work. “As we continue to map the RNA modification landscape, we expect many more discoveries with meaningful implications for infectious disease, antimicrobial resistance, and fundamental biology.”

Bacteria can develop resistance to antibiotics using various strategies, many of which depend on the bacteria’s ability to regulate which proteins are made, when they are made, and how accurately they are produced — whether by pumping drugs out of their cell, creating enzymes that break down drugs, or developing new cell processes to avoid the antibiotics’ target.

To build these proteins, bacteria rely on RNA molecules to read genetic instructions and direct protein production. Among these RNA molecules are transfer ribonucleic acid (tRNAs), a specialized class of RNA that acts as molecular delivery vehicles bringing chemical “stickers” to help bacteria control how proteins are made in response to stress and changing conditions such as exposure to antibiotics.

In the open-access paper, “Pyridoxal phosphate-dependent biosynthesis of aminovaleramide by AvaS in tRNA,” published Sept. 9 in Nature Chemical Biology, the researchers described their discovery of the new enzyme and identified it as being responsible for creating a tRNA chemical modification known as aminovaleramide cytidine (ava²C) in Pseudomonas aeruginosa, a harmful bacterium responsible for a range of serious human infections such as pneumonia and sepsis. While ava²C had previously been detected in several bacteria and plants, the enzyme responsible for producing this modification was previously unknown.

Using SMART AMR’s high-throughput liquid chromatography-tandem mass spectrometry (LC-MS/MS)-based RNA modification profiling platform, the team systematically screened thousands of P. aeruginosa mutants and discovered AvaS. The researchers also confirmed the presence of ava²C in other organisms, including the bacteria Acinetobacter baumannii and Vibrio cholerae, as well as the plant Arabidopsis thaliana.

The research revealed that AvaS uses PLP, a vitamin B6 derivative, to convert a known modification, lysidine (k²C), into ava²C; marking the first time that a PLP-dependent enzyme has been linked to tRNA modification. Traditionally, PLP-dependent enzymes have only been associated with amino acid metabolism and related biochemical pathways. 

The research findings revealed a few important insights about PLP-dependent enzymes. First, the discovery establishes PLP-dependent enzymes as a previously unrecognized class of tRNA-modifying enzymes, expanding the known chemical mechanisms, such as methylation, thiolation, and isomerisation, that bacteria use to regulate protein production. Second, it reveals an entirely new biological function of PLP-dependent enzymes, demonstrating that they can directly modify tRNA in addition to their well-established roles in metabolic processes.

The research also found that ava²C changes how bacteria read genetic codes, enabling the bacteria to produce protein faster and more efficiently while helping them adapt to metabolic and oxidative stress.

“Our discovery has revealed, for the first time, that PLP-dependent enzymes can directly modify tRNA, expanding our knowledge and understanding of RNA-modifying chemistry,” says Jingjing Sun, research scientist at SMART AMR, first author, and co-corresponding author of the paper. “This opens up new avenues for studying bacterial adaptation and developing new and more effective strategies to overcome drug-resistant bacteria.”

Building on this discovery, the SMART AMR team plans to investigate how ava²C affects bacterial stress responses and metabolism and explore how the modification can be disrupted or prevented. Understanding this process could uncover new ways to fight harmful bacteria and develop future antimicrobial therapeutics. With ava²C also being observed in plants, future studies could explore whether other living organisms use similar biological tools to produce certain chemical modifications and how ava²C influences the way proteins are built beyond bacteria.

More broadly, this work highlights the strength of SMART AMR’s first-of-its-kind epitranscriptomics platform as a powerful engine in discovering more unknown RNA-modifying enzymes at scale. This capability could also support biotechnology and pharmaceutical researchers in finding new drug targets and developing better treatments, particularly as bacteria continue to develop resistance against existing drug treatments.

The research conducted at SMART is supported by the National Research Foundation Singapore under its Campus for Research Excellence and Technological Enterprise program.

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A new understanding of how enzymes influence bacterial protein production

Antimicrobial resistance is one of the most pressing global health and development challenges of our time. Bacteria and other pathogens are rapidly developing resistance to existing treatments, making infections harder to treat. Without new approaches, minor inconveniences today, such as routine surgeries or even a paper cut, could become life-threatening tomorrow. 

Now, an international group of scientists reports the discovery of aminovaleramididine synthetase (AvaS), the first identified pyridoxal phosphate (PLP)-dependent enzyme responsible for producing a chemical modification linked to how bacteria respond to metabolic stress. This discovery sheds new light on how bacteria use RNA modification to control protein production, opening new avenues to study bacterial adaptation and identify future targets and better strategies for developing antimicrobial therapeutics. 

The work was led by researchers from the Singapore-MIT Alliance for Research and Technology’s Antimicrobial Resistance interdisciplinary research group (SMART AMR), alongside collaborators from MIT, Nanyang Technological University in Singapore, and institutions in the United States, Poland, and France.

“While many RNA modifications have been known for decades, researchers are still uncovering the full extent of their roles. The discovery of AvaS opens a previously unknown chapter in RNA biology and is an important step forward in our understanding of processes relevant to antimicrobial resistance,” says Professor Peter Dedon, co-lead principal investigator at SMART AMR, professor of biological engineering at MIT, and co-corresponding author of a new paper on the work. “As we continue to map the RNA modification landscape, we expect many more discoveries with meaningful implications for infectious disease, antimicrobial resistance, and fundamental biology.”

Bacteria can develop resistance to antibiotics using various strategies, many of which depend on the bacteria’s ability to regulate which proteins are made, when they are made, and how accurately they are produced — whether by pumping drugs out of their cell, creating enzymes that break down drugs, or developing new cell processes to avoid the antibiotics’ target.

To build these proteins, bacteria rely on RNA molecules to read genetic instructions and direct protein production. Among these RNA molecules are transfer ribonucleic acid (tRNAs), a specialized class of RNA that acts as molecular delivery vehicles bringing chemical “stickers” to help bacteria control how proteins are made in response to stress and changing conditions such as exposure to antibiotics.

In the open-access paper, “Pyridoxal phosphate-dependent biosynthesis of aminovaleramide by AvaS in tRNA,” published Sept. 9 in Nature Chemical Biology, the researchers described their discovery of the new enzyme and identified it as being responsible for creating a tRNA chemical modification known as aminovaleramide cytidine (ava²C) in Pseudomonas aeruginosa, a harmful bacterium responsible for a range of serious human infections such as pneumonia and sepsis. While ava²C had previously been detected in several bacteria and plants, the enzyme responsible for producing this modification was previously unknown.

Using SMART AMR’s high-throughput liquid chromatography-tandem mass spectrometry (LC-MS/MS)-based RNA modification profiling platform, the team systematically screened thousands of P. aeruginosa mutants and discovered AvaS. The researchers also confirmed the presence of ava²C in other organisms, including the bacteria Acinetobacter baumannii and Vibrio cholerae, as well as the plant Arabidopsis thaliana.

The research revealed that AvaS uses PLP, a vitamin B6 derivative, to convert a known modification, lysidine (k²C), into ava²C; marking the first time that a PLP-dependent enzyme has been linked to tRNA modification. Traditionally, PLP-dependent enzymes have only been associated with amino acid metabolism and related biochemical pathways. 

The research findings revealed a few important insights about PLP-dependent enzymes. First, the discovery establishes PLP-dependent enzymes as a previously unrecognized class of tRNA-modifying enzymes, expanding the known chemical mechanisms, such as methylation, thiolation, and isomerisation, that bacteria use to regulate protein production. Second, it reveals an entirely new biological function of PLP-dependent enzymes, demonstrating that they can directly modify tRNA in addition to their well-established roles in metabolic processes.

The research also found that ava²C changes how bacteria read genetic codes, enabling the bacteria to produce protein faster and more efficiently while helping them adapt to metabolic and oxidative stress.

“Our discovery has revealed, for the first time, that PLP-dependent enzymes can directly modify tRNA, expanding our knowledge and understanding of RNA-modifying chemistry,” says Jingjing Sun, research scientist at SMART AMR, first author, and co-corresponding author of the paper. “This opens up new avenues for studying bacterial adaptation and developing new and more effective strategies to overcome drug-resistant bacteria.”

Building on this discovery, the SMART AMR team plans to investigate how ava²C affects bacterial stress responses and metabolism and explore how the modification can be disrupted or prevented. Understanding this process could uncover new ways to fight harmful bacteria and develop future antimicrobial therapeutics. With ava²C also being observed in plants, future studies could explore whether other living organisms use similar biological tools to produce certain chemical modifications and how ava²C influences the way proteins are built beyond bacteria.

More broadly, this work highlights the strength of SMART AMR’s first-of-its-kind epitranscriptomics platform as a powerful engine in discovering more unknown RNA-modifying enzymes at scale. This capability could also support biotechnology and pharmaceutical researchers in finding new drug targets and developing better treatments, particularly as bacteria continue to develop resistance against existing drug treatments.

The research conducted at SMART is supported by the National Research Foundation Singapore under its Campus for Research Excellence and Technological Enterprise program.

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Fueling a return journey from Mars

When Lanie McKinney was 3 years old, her parents stopped at a massive meteor crater during a road trip through the U.S. Southwest. As they prepared to leave, McKinney began to protest.

“I want to wait here for the next one,” she told them.

She didn’t yet understand that another meteor wasn’t likely to land in exactly the same spot. But the story, which her parents still tell, captures a fascination that has remained with McKinney throughout her life.

“I just always remember being captivated by space and what is out there,” she says.

Today, McKinney is entering her fifth year as a PhD candidate at MIT, where she works in the Aerospace Plasma Group with Esther and Harold E. Edgerton Associate Professor Carmen Guerra-Garcia. McKinney’s research focuses on developing technologies that could help humans explore Mars.

One of the challenges of sending humans to the Red Planet is figuring out how to supply them once they arrive — including how to enable their journey back home. Rather than transporting everything from Earth, McKinney is interested in using the resources already available on the planet, a concept known as in-situ resource utilization, or ISRU.

“If we don’t build gas stations on Mars, it will be very difficult to get humans back to Earth,” she says. “We’re going to need some way to produce the propellant on site.”

McKinney’s research uses cold plasma to convert carbon dioxide, which is abundant in the martian atmosphere, into oxygen and carbon monoxide, a technology that could eventually be used to produce life support and propellant on Mars. 

An Oklahoma native, McKinney earned her bachelor’s at the University of Tulsa, where she studied physics and applied mathematics. She had initially expected to pursue astrophysics, but a summer research internship at the University of Colorado at Boulder introduced her to plasma physics through a project involving dusty plasmas in the lunar environment. 

“I thought it was an incredibly interesting problem,” she says. 

At MIT, McKinney has developed a small reactor that can convert carbon dioxide into oxygen and other products. The challenge now is separating out the oxygen before it recombines.

“We can actually perform the conversion step really well,” she says. “But what happens in a plasma is we convert it, and then we get a mixture that needs to be separated.”

Her current work pairs the plasma reactor with an oxygen-selective membrane designed to extract oxygen rapidly. The integration process isn’t well-understood, leaving McKinney and her colleagues with questions about how the reactive plasma environment will affect the membrane.

“We are not entirely sure what we will see,” she says.

For McKinney, the possibility of connecting laboratory experiments to future human missions is what makes the work particularly rewarding.

“I get to work in a really cool lab and develop exciting experiments,” she says. “I get ownership over an entire experimental system, and then I get to connect that to performance requirements for a future Mars system. That’s just the dream.” 

That same philosophy has shaped McKinney’s work beyond her thesis. Through MIT’s Space Resources Workshop, she has participated in NASA competitions focused on sustaining humans in space. Her first competition involved designing a self-sustaining Mars mission for 10 years.

“I had no clue what was going on,” she says. “I  didn’t know anything about space systems. So, my mentality was, let me jump in and learn.”

She later co-led MIT’s CERBERUZ team for NASA’s LunaRecycle Challenge, which asked teams to develop ways to recycle waste on missions to the moon and deep space. The MIT team recently won first prize in Phase 2, receiving $775,000 in awards for a system that grinds mixed trash into powder that can be reused via injection molding to make spare parts and 3D-printing filament. 

Another project McKinney enjoyed brought together engineers and architects through MAS.S66/4.154/16.89 (Space Architecture) to tackle a different problem: how to protect lunar habitats from radiation using only resources available on the moon. The students’ solution was to produce cast bricks from lunar regolith that could be stacked without mortar or another binder. For McKinney, the project demonstrated the value of bringing together people with different expertise.

“The kinds of innovative solutions that can be discovered when you work on a team that brings together different expertise and experiences was one of the project’s major takeaways,” she says.

The experience reflects a broader lesson McKinney has taken from MIT: Research may involve focused individual work, but solving the problems of human space exploration will require collaborations across disciplines.

“I feel like I have learned so much from being a part of these different teams,” she says. 

McKinney sees that collaboration as essential to the future she hopes to help build. Reaching the Moon and Mars is only the first step: “What comes next is building up a permanent presence so that we can do amazing science and be really effective at exploration,” she says.

McKinney’s fascination with exploration extends beyond her research. She is an avid hiker and mountaineer, having grown up hiking with her family in the Rockies. She recently completed a mountaineering course in Alaska and summited Mount Baker in the Cascade Range. She sees a connection between those adventures and the curiosity that first drew her to space.

“I love to explore and go on adventures,” she says. “And space is the ultimate thing you could explore.”

That curiosity has also shaped how McKinney approaches her work. When she arrived at MIT from the University of Tulsa, she initially felt intimidated.

“I thought that it was a fluke that I’d gotten in,” she says. “I was very nervous that I was not going to measure up to the environment.”

Over time, she learned to approach unfamiliar problems by asking questions and committing fully to whatever interested her.

“If something interests you, try it and go all in,” she says.

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