Biochemistry professor Robert Landick has been elected to the American Academy of Arts and Sciences, one of three faculty from the University of Wisconsin–Madison that make up the 2018 class of members.
Founded in 1780, the American Academy honors leaders in science, the arts, business and American life. Other members elected this year include former president Barack Obama, Supreme Court Justice Sonia Sotomayor and actor Tom Hanks. Alexander Hamilton, Charles Darwin and Martin Luther King Jr. are among those previously recognized by the Academy.
“It's both humbling and an exceptional honor to be included among such an illustrious group of people,” Landick says. “The real accomplishment, though, belongs to the students and researchers who have worked with me over the years to figure out mechanisms of gene expression. Without their spectacular accomplishments, there would be little for the American Academy of Arts and Sciences to recognize.”
Read more about Landick's award and research at the link below.
The award is supported by an educational development fund created to honor CALS Dean Glenn S. Pound upon his retirement in 1979. It is given to honor an outstanding, early-career CALS research scientist and to promote continued excellence in research.
“It is a great honor to be recognized with this award for young investigators,” Hoskins says. “A lot of credit for this goes to the wonderful students and scientists who have worked in my laboratory as well as my mentors and collaborators here at UW–Madison.”
Read the rest of this story at the link below.
The RNA transcripts of virtually all human genes must be processed by one cellular machine: the spliceosome. The mind-boggling array of proteins and RNAs that make up the spliceosome allow it to control how genes are expressed. Many researchers are interested in the dynamic interplay between these components of the spliceosome and how they evolved, likely from a parasitic RNA that invaded eukaryotic cells at around the same time eukaryotic and bacterial cells became distinct from one another approximately two billion years ago.
The spliceosome is also a reason that complex organisms like animals and humans can exist. Through splicing, the cell is able to get several different transcripts out of just one gene, meaning a more diverse array of proteins can be made from a relatively small amount of DNA. This creates evolutionary diversity much more rapidly than other mechanisms, allowing complex organisms to evolve more quickly.
Researchers chip away at the spliceosome and its dynamic components by several approaches. One approach, facilitated by recent advances in cryo-electron microscopy (cryo-EM), involves determining three-dimensional structures of fully assembled spliceosomes. Another approach involves studying smaller sub-complexes, which allows more detailed views of protein-RNA interactions and also provides tractable in vitro systems for testing specific hypotheses about function.
The laboratories of biochemistry professor Sam Butcher and biomolecular chemistry professor David Brow at the University of Wisconsin–Madison recently took the latter approach to hone in on a protein called Prp24 and a seven-protein ring called the Lsm2-8, both of which recruit a critical RNA called U6 into spliceosomes. In their newest study published in Nature Communications on May 1, 2018 they reported for the first time the structure of these eight proteins interacting with the U6 RNA.
Read the rest of this story at the link bleow.
People who eat a high-fat, high-sugar “Western” diet typically exhibit physiological changes associated with type 2 diabetes. However, not everyone responds the same way to the Western diet; genetics plays a strong role in determining one’s susceptibility to develop diabetes.
In type 2 diabetes, islet cells in the pancreas can’t produce enough insulin and other hormones that control blood glucose (sugar). If left uncontrolled, this leads to dangerously high levels of glucose in the blood that may result in tissue and organ damage and early death.
So, finding genes that promote insulin secretion could be a valuable source of treatment strategies for type 2 diabetes. And that’s just what researchers in the lab of biochemistry professor Alan Attie at the University of Wisconsin–Madison and collaborators at The Jackson Laboratory discovered when comparing the genetic variations associated with type 2 diabetes in humans with those of a special, genetically diverse mouse population fed on a diet high in fat and sugar.
The work, published in the journal Genetics, is the first to show how a Western-style diet alters the regulation of genes in the pancreatic islets of mice. It also demonstrates that the Diversity Outbred (DO) mouse population can stand in for humanity in laboratory studies of genetic risk variants found in human genome-wide association mapping.
This press release was written by Joyce Dall'Acqua Peterson of The Jackson Laboratory and was originally published on their news site.
To read more about this work, see the link below.
Three Integrated Program in Biochemistry (IPiB) students are recipients of 2018 National Science Foundation Graduate Research Fellowship awards.
The NSF Graduate Research Fellowship Program recruits high-potential scientists and engineers and supports their graduate research training in STEM fields. Fellows receive three years of financial support through a $34,000 annual stipend and $12,000 education allowance. More than 12,000 students from across the United States applied, with 2,000 receiving awards.
To see a list of all UW–Madison students who received NSF fellowships, see the link below.
The University of Wisconsin–Madison Department of Biochemistry will welcome Elizabeth Wright in July as a faculty member and director of the department’s newly established cryo-electron microscopy (cryo-EM) facility.
Wright is an expert in cryo-EM, a technique able to obtain atomic or near-atomic level resolution images of biological molecules by imaging with electrons. It is a burgeoning technology that can help UW–Madison researchers make significant new contributions to many areas of structural biology, including enzymology, virology, cell biology, and medicine.
“I am very excited to be joining the department to develop this technology at UW–Madison,” says Wright, who will also be an affiliate of the Morgridge Institute for Research. “In the fields of fundamental biochemistry and structural biology, the department is one of the strongest in the country. I was drawn to UW–Madison by the vision the department has for this facility. We are not just thinking about the present but about the next decade and beyond by establishing an advanced cryo-EM resource and building a community to push forward scientific understanding across many biological research areas by using cryo-EM.”
To read more about Wright and her work, see the link below.
Think of neurons like cities, which need to be able to transport goods and services throughout themselves. In cities this is done on highways by cargo trucks. In neurons it’s done on microtubules by motor proteins. To direct traffic, cities have signals like lights and road signs, while in neurons these signals are thought to come in the form of post-translational modifications.
These modifications on the microtubules are hypothesized to ensure that cargo in these neurons gets to the right place at the right time. The lab of assistant professor Jill Wildonger at the University of Wisconsin–Madison Department of Biochemistry studies these modifications and their impact on the transport of cargo. New research from the Wildonger Lab led by postdoctoral scholar Brian Jenkins investigated a particular post-translational modification, using a new approach to find that researchers’ assumptions about the modification might not have been as correct as once thought. Their research was recently on the cover of the Journal of Cell Science.
Read about this work at the link below.
University of Wisconsin–Madison graduate programs in biochemistry are once again ranked among the nation’s best in the 2019 edition of U.S. News & World Report’s “Best Graduate Schools.” The university ranks 8th in the nation in the biochemistry specialty category under chemistry.
The UW–Madison Integrated Program in Biochemistry (IPiB) is the joint graduate program of the Department of Biochemistry in the College of Agricultural and Life Sciences and the Department of Biomolecular Chemistry in the School of Medicine and Public Health. The program is home to around 100 graduate students and 52 world-class faculty pursuing cutting-edge research in all areas of biochemistry.
“It is great to see this recognition of our program,” says biochemistry professor Ivan Rayment, director of graduate studies and the chair of IPiB’s steering committee. “It is testament to the quality of our students and faculty and their commitment to research and training. You will find our graduates all over the world in a host of professional activities. Ultimately they are the best measure of our success.”
IPiB faculty make contributions to biology and chemistry, researching a diverse array of biological processes including plant flowering; protein structure; membrane trafficking and transport; vitamin and hormone action; signal transduction mechanisms; RNA processing; DNA replication, recombination and transcription; cell division and differentiation; viral replication and transcription; and animal development.
“The fact that so many of the graduate programs at UW–Madison are ranked is a testament to our senior leadership, who foster an environment of academic excellence; our outstanding faculty and staff, who lead cutting-edge research programs; and our creative students, who bring curiosity and vibrancy to address the most important questions that society faces today,” says William Karpus, dean of UW–Madison’s Graduate School.
This story was adapted from a press release by Käri Knutson of University Communications that was originally published on the UW–Madison news site.
Biochemistry professor Richard Amasino has been awarded a Wisconsin Alumni Research Foundation (WARF) Named Professorship. Support for the award is provided by the University of Wisconsin–Madison Office of the Vice Chancellor for Research and Graduate Education (VCRGE) with funding from WARF.
“It's an honor to be recognized with this award,” Amasino says. “Because it’s a university-wide award it is even more humbling to receive it given all of the great faculty at this outstanding university.”
Amasino has a long history of extraordinary research, teaching, and service to the university, state of Wisconsin, and the worldwide scientific community. His research as a plant biochemist has combined biochemistry, molecular biology, and genetic approaches to investigate the molecular basis of how plants sense the seasonal cues of changing day-length and temperature and use these cues to flower at the appropriate time of year. He also participates in the research program of the Department of Energy-funded Great Lakes Bioenergy Research Center (GLBRC), studying how to increase yield of grasses used for biomass production, and for the first 10 years of the GLBRC served on the management team that oversaw the research portfolio.
Read more about Amasino's work at the link below.
Proteins are an impressive bunch. Starting with amino acids as their basic building blocks, these complex molecules fold into intricate 3D structures and control just about every biological process that keeps us alive.
Phil Romero wants to understand how proteins accomplish that job so that he can eventually apply their power to important problems in medicine, agriculture, chemistry and bioenergy.
“Describing how proteins perform a vast array of biological functions is tremendously challenging for two reasons,” says Romero, an assistant professor of biochemistry at the University of Wisconsin-Madison. “One, they are highly dynamic molecules that constantly change their shape; and two, their properties emerge from the collective behavior of many interacting components.”
So instead of relying on a bottom-up approach that uses the laws of physics to predict biological behavior, Romero, who has an affiliate appointment with the Department of Chemical and Biological Engineering, is betting on the top-down approach: learning how protein sequence translates into function by analyzing massive data sets.
“Our ability to generate, store and analyze biological data has exploded during the last decade,” Romero says. “That’s why data-driven approaches are playing an increasingly important role in biological discovery and engineering.”
To read more about Romero's work, see the link below.
The Department of Biochemistry and Department of Biomolecular Chemistry invite you to the 39th annual Steenbock Symposium on May 29-June 2, 2018. Registration is now open, and early discounted registration ends April 15.
This year’s symposium, entitled “Iron-Sulfur Proteins—Biogenesis, Regulation and Function,” will bring together scientists from across UW–Madison, the country, and the globe to discuss this unique class of proteins.
Patricia Kiley, professor and chair of Biomolecular Chemistry, and John Markley, biochemistry professor and director of the National Magnetic Resonance Facility at Madison (NMRFAM), are serving as this year’s organizers.
“This is really the only meeting on this class of proteins out there,” Kiley says. “We have held a meeting on iron-sulfur proteins in different locations in the United States and Europe for several years now — this year under the banner of Steenbock Symposium at UW–Madison — and it’s a unique and exciting event for those who work in this field. This is actually the second time that UW–Madison has hosted the meeting and reflects our rich history of investigations of Fe-S proteins beginning with Helmut Beinert, who pioneered spectroscopic methods that enabled their study.”
Twenty speakers are slotted for the event, and an additional 20 will be promoted from submitted abstracts. For more information on the symposium and to register, go to this link: https://biochem.wisc.edu/symposia/steenbock/39th.
The Steenbock Symposium is supported by the Steenbock Endowment to honor Professor Harry Steenbock’s work as a distinguished Biochemistry faculty member, whose contributions spanned many areas of nutrition and biochemistry.
Integrated Program in Biochemistry (IPiB) graduate student Mark Klein and IPiB faculty member Peter Lewis took to the ice during the Wisconsin Badgers vs. Penn State Nittany Lions hockey game on Saturday, Jan. 27 to receive awards to help fund their cancer research.
Klein is in the lab of biomolecular chemistry professor John Denu and Lewis is an assistant professor of biomolecular chemistry. Both labs are part of the Wisconsin Institute for Discovery and affiliated with the University of Wisconsin Carbone Cancer Center.
The awards were sponsored by The Ride, a fundraising event hosted by the Carbone Cancer Center. In its second year, it drew more than 1,250 bike riders to the roads of eastern Dane County in September of 2017 to raise money for cancer research. One hundred percent of the $352,000 raised went back to cancer research at the university in the form of 14 research awards. Awardees were invited onto the ice to be recognized.
“It was really exciting to win this award and get acknowledged at the hockey game,” says Klein, who has already signed up to participate in the next Ride in September 2018. “We spend a lot of time hunkered down in our labs but getting this award helps us step back and see that our work is novel and meaningful. It was great to have our work on cancer be recognized this way in front of an entire hockey stadium.”
Klein studies a particular protein that has been implicated in many forms of cancer. Research shows that in ovarian cancer cells, the protein is deficient but when it’s overexpressed in the cells, the protein can prevent cancer. His next step is seeing if he can find a synthetic molecule that can be used to mimic this overexpression and hence possibly help with preventing cancer. However, he says this work also provides an important understanding of the basic mechanisms and functions behind this protein and any synthetic compounds he studies.
“Mark’s research is focused on understanding how a tumor suppressor enzyme called SIRT6 can be activated by endogenous molecules and on developing a synthetic compound that could function similarly,” Denu says. “Mark has a unique skill of fostering collaborations with other researchers on this campus, including Professor Weiping Tang who is synthesizing potential compounds.”
Lewis studies how protein molecules that “spool” the DNA in cells can regulate cellular function and influence how cancer cells grow and respond to treatment. These protein molecules called histones keep the DNA wrapped up in an inaccessible ‘off’ state and releases it when certain genes are needed by the cell. Research shows that specific mutations to the histones are drivers of certain types of pediatric cancers in humans.
The Lewis Lab is trying to figure out how and why this happens. They’ve found that specific “oncohistone” mutations drive some pediatric cancers by transforming histone proteins into potent inhibitors of gene regulatory processes. Their work explores fundamental questions in biology but also clinically relevant ones.
“It was a great surprise and honor to be selected as a Ride Scholar,” says Lewis, who will also participate in the 2018 Ride. “You see the huge amount of work that goes into organizing events like this and the effort all the bikers put in. It’s so great to know their hard work is going directly to cancer research. It’s very humbling to have received an award.”
A new chair at the Morgridge Institute for Research takes aim at osteoarthritis, a debilitating and painful disease that affects more than 27 million Americans. Currently, osteoarthritis is largely treated with palliative care to help patients alleviate their symptoms.
“I think because arthritis is life-altering, not life-threatening, it doesn’t attract the research dollars required to find a solution,” says Peggy Pyle. “It’s time to change that!”
And Peggy knows. Since she was diagnosed with osteoarthritis, she’s been shocked at the lack of research into prevention and irradication of the disease. Treatment options are limited to medications like NSAIDs or joint replacement with no way to stop osteoarthritis’s progression.
Peggy’s commitment to battling the disease has only increased since her husband Tom was diagnosed with arthritis and underwent a hip replacement.
Now with support from the Thomas and Margaret Pyle Chair, which honors Tom’s longtime service on the Wisconsin Alumni Research Foundation Board of Trustees, there’s a new commitment to tackling osteoarthritis at the University of Wisconsin-Madison.
Joshua Coon, a professor of chemistry and biomolecular chemistry and Morgridge Institute affiliate, is the inaugural recipient of the chair. The Coon Lab specializes in creating and applying high-powered must-have technologies that help scientists answer biomedical questions with applications for human health.
“We hope to accelerate technology and accelerate all areas of biological research,” he says. “I really consider our team ‘technologists.’ We are building and developing new tools to measure biomolecules.”
Coon is a renowned innovator of mass spectrometry technology with more than 100 research collaborations across UW-Madison and the world, including the Morgridge Metabolism Initiative directed by Dave Pagliarini, the Great Lakes Bioenergy Research Center and ongoing research supported by the National Institutes of Health to identify molecular markers of Alzheimer’s disease.
For more of this story, see the link below.
Science is a visual enterprise. Scientific imagery created with microscopes, telescopes, cameras and scanners makes even parts of the world that our eyes can’t perceive visible, understandable and often beautiful.
To recognize the visual and exploratory value of scientific imagery, the 8th annual Cool Science Image Contest is soliciting the best images from members of the University of Wisconsin–Madison community.
Sponsored by Promega Corp. with additional support from the UW–Madison Arts Institute and DoIT Digital Publishing and Printing Services, the Cool Science Image Contest offers an opportunity to show off compelling science images made by students, staff or faculty.
To read more about the contest rules and how to submit an entry see the link below.
“It’s exciting to be invited to be part of this group, but what’s more exciting is that the rest of the researchers in this group are phenomenal,” Raman says. “I know some of them personally and they really cover the entire spectrum of research and represent the next big things in biochemistry. I’m happy to be a part of an amazing group of people that I respect.”
For the special issue, he wrote a perspective piece on understanding and designing allosteric proteins, a major part of his research lab. These proteins are mysterious in how they function but play major roles in cellular function, such as signaling, gene regulation, and transport.
Read more about Raman and his research at the link below.
The phrase seeing is believing doesn’t just apply to supernatural phenomenon; biochemists often say the same thing when imaging proteins or other molecules for the first time.
Imaging is a powerful tool in many biochemists’ repertoire. The Department of Biochemistry at the University of Wisconsin–Madison is home to a large collection of equipment and facilities, including the Biochemistry Optical Core (BOC) and upcoming UW–Madison cryo-electron microscopy (cryo-EM) facility, that allows scientists to pursue their many imaging endeavors. The department’s goal is simple: to provide faculty, researchers, and students from the department and all across campus with access to these resources and the training to operate them, even if they’ve never used them before.
Elle Kielar-Grevstad, the director of the BOC and supervisor to the department’s core facility staff, serves to promote and facilitate the department’s mission by helping researchers with their light and fluorescent microscopy needs.
“Imaging is really capturing a state of being,” she says. “That can mean a lot of things depending on what resolution you require. Whether you are looking at a whole animal, a tissue, a single cell, or a single protein, you’re still capturing a state of being, or in many cases multiple states of being. Your research question will determine the resolution requirements and that in turn dictates what type of equipment you need. The great thing about all the core facilities at Biochemistry is that we can likely help you meet your imaging or experimental needs, and if we can’t, it is our job to connect you with others on campus that can.”
Learn more about Biochemistry' imaging capabilities and how students can access these resources at the link below.
Coenzyme Q (CoQ) is a vital cog in the body’s energy-producing machinery, a kind of chemical gateway in the conversion of food into cellular fuel. But six decades removed from its discovery, scientists still can’t describe exactly how and when it is made.
Dave Pagliarini, associate professor of biochemistry and Intergrated Program in Biochemistry faculty member, says the list of unknowns is daunting. How does it migrate around in the cell? How does it get used up and replenished? What genes and proteins are responsible for CoQ dysfunction? Why does its presence decline as people age?
Pagliarini, also director of metabolism at the Morgridge Institute for Research, and his group are dedicated to chipping away at many of these knowledge gaps in CoQ production and in understanding the role of CoQ deficiency in human disease. CoQ deficiencies are implicated in scores of diseases, including liver and lung failures, muscle weakness, deafness and many brain disorders such as Parkinson’s and cerebellar ataxia. The coenzyme is almost exclusively produced within the body and is often very difficult to replenish through nutritional supplements.
Against this backdrop, the Pagliarini lab is developing new tools to shed light on CoQ function, primarily by finding and defining proteins that have a direct link to the chemical. In the past month, Pagliarini’s team has published three collaborative papers that gather multiple layers of information on cells where proteins have been manipulated.
“A fundamental challenge in biology lies in connecting the many ‘orphan’ proteins in our cells with specific biological processes, such as CoQ biosynthesis,” says Pagliarini. “Once we have a handle on their functions, a second challenge is to devise ways to manipulate the activity of these proteins, pharmacologically or otherwise, to control key biological processes and, ultimately, improve health.”
Research published in the journals Cell Systems (Dec. 13), Molecular Cell (Dec. 7) and Cell Chemical Biology (Nov. 29) all reveal new clues to coenzyme Q production and function.
Read about the findings from these three papers at the link below.