Highlights:
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Elizabeth Vierling Chosen as Spotlight Scholar
Distinguished Professor Elizabeth Vierling, a leader in research on heat stress in plants, is being recognized as a Spotlight Scholar. Vierling studies molecular chaperones, molecules necessary for protein folding, transport, modulation and regulation, and also important for plant stress tolerance. [More]
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Danny Schnell Given Award at Faculty Convocation
BMB Professor Danny Schnell is one of five faculty on campus recognized at Faculty Convocation on October 4th. He was presented the Award for Outstanding Accomplishments in Research and Creative Activity for his work in organelle biogenesis and protein import into plant chloroplasts. He is currently the principal investigator on a $4.2 million dollar Department of Energy grant to develop a dedicated high-value biofuels crop. [More]
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New Life Science Laboratories Opens!
A number of very excited BMB faculty and their lab members, along with faculty from five other departments on campus, moved their labs and offices into Phase I of the new Life Science Laboratories (LSL) on Thatcher Road, behind the ISB. The building contains state-of-the-art open-format laboratories designed to foster collaboration among research groups, along with specialized equipment rooms, faculty offices, conference rooms and computing areas. BMB research groups now located in the LSL include the Chien, Gershenson, Gierasch, Hebert, Ma, Normanly, Schnell, Vierling and Wang labs, along with the Mass Spectrometry Facility.
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Microbial Temper Tantrums: Stressed Bacteria Destroy Proteins
As published August 1 in Cell, scientists from the Chien lab, along with the Laub lab at MIT, showed that bacteria respond to stress such as high temperatures by destroying DNA replication proteins. The destruction signal turns out to be the buildup of proteins that were misfolded because of the stress. High amounts of misfolded proteins trigger the protease to destroy an otherwise normal protein needed for DNA replication. Because destruction of this protein stops cell growth, cells don't waste resources before the stress ends. When the stress passes, the number of misfolded proteins drops, DNA replication begins and cells quickly restart growth. Stress and protein misfolding are a universal part of life, so understanding how simple bacteria deal with this kind of stress will help us understand how our cells do as well. This work was funded by the National Institutes of Health, the Howard Hughes Medical Institute and UMass Amherst. [Read more]
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Lila Gierasch Selected to Receive Mildred Cohn Award
Distinguished Professor Lila M. Gierasch has been selected to receive the 2014 Mildred Cohn Award in Biological Chemistry, given annually by the American Society for Biochemistry and Molecular Biology (ASBMB). The award honors the pioneering scientific accomplishments and the spirit of Mildred Cohn, the first female president of the ASBMB. It recognizes and honors scientists at all stages of their careers who have made substantial advances in understanding biological chemistry using innovative physical approaches.
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Chase and Maher Publish New Knockdown Strategy
Double-stranded RNA interference (dsRNAi) targets gene-specific mRNAs for destruction and is a powerful approach for rapidly assessing gene function. Recently Assistant Professor Dan Chase and Postdoctoral Researcher Kathryn Maher developed a novel method for cell type-specific knockdown of gene expression in C. elegans which overcomes limitations of previous methods. This new approach is stably inherited, absolutely cell-autonomous and can also be controlled temporally, allowing the timing of gene knockdown to be controlled by the investigator. Using this new knockdown approach, protein function can now be investigated with single-cell resolution in live, behaving animals. [Read more]
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Chien Lab Reports Finding Bacterial "Needles in a Haystack"
Energy-dependent proteases are responsible for the removal of proteins from cells, a process required for normal growth, division and differentiation to take place, but which proteins are degraded, and when, remains unclear. Researchers in the Chien lab recently used a combination of biochemistry and mass spectrometry to 'fish out' proteins targeted for degradation during bacterial development. In recently published work, they report over 100 new candidate proteins that cover all aspects of bacterial growth, including DNA replication, transcription, and cytoskeletal changes. Eliminating the ability to degrade one of these new targets makes the bacteria unable to differentiate properly, thereby dramatically affecting bacterial development. Because these developmental changes are essential for bacteria to invade a host, these insights could identify new drug targets in antibiotic-resistant bacteria, a growing human health concern. [Read more]
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Heuck Lab Contributes to Development of New Product
Prof. Alejandro Heuck, along with Dr. Nagendra Yadava of the Pioneer Valley Life Sciences Institute, contributed to the development of the XF Plasma Membrane Permeabilizer (PMP), a product licensed to Seahorse Biosciences. The product is a reagent which enables a new method of measurement of mitochondrial function, allowing development and testing of drugs for treatment of diseases including diabetes and heart failure. [Read more]
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Cannon Lab Publishes Report of Alternate Gene Expression in Arabidopsis
Research Associate Professor Maura Cannon, along with members of her lab and collaborators at the Noble Foundation, Ardmore, OK, and at Ohio University, Athens, OH, report on a cell wall mutant in Arabidopsis that rescues itself and undergoes a reversion to a normal phenotype by switching to an alternate gene expression landscape. This allows apparently normal growth and produces a fertile plant. [Read more]
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Essential Role for Heat Shock Protein 90 (Hsp90C) Elucidated
Recent studies by Professor Danny Schnell and Postdoctoral Associate Hitoshi Inoue, published in the current issue of the Proceedings of the National Academy of Sciences, have identified a molecular chaperone, Hsp90C, which plays a key role in determining the fate of photosynthesis proteins. Hsp90C appears to participate as part of a complex chaperone network that maintains the proper transport, folding and assembly of the photosynthetic apparatus. The function of the chaperone network appears to be essential for plant function, and especially in plant seedlings when the photosynthetic machinery is being built and plants transition from their dependence on seed reserves to producing their own energy. [Read more]
