Eva Nogales, a senior faculty scientist in the Molecular Biophysics and Integrated Bioimaging (MBIB) Division, was appointed as a foreign member attached to the Natural Sciences Section of the Royal Academy of Exact, Physical, and Natural Sciences of Spain. The Royal Academy, founded in 1847, is tasked with promoting study and research in the mathematical, physical, chemical, geological, and biological sciences, as well as disseminating the knowledge gained thereby. It is made up of a maximum of 72 permanent members, 144 corresponding members, and supernumerary members and foreign members. Nogales, who is also a Howard Hughes Medical Institute (HHMI) investigator and professor at UC Berkeley, obtained her bachelor’s degree in physics from the Universidad Autonoma de Madrid in Spain. Her research specialty involves using electron microscopy (EM) and image analysis, as well as biochemical and biophysical assays to gain mechanistic insights into crucial molecular processes in the life of eukaryotic cells.
New Insights into a Gene Silencing Complex
The multi-protein structure polycomb repressive complex 2 (PRC2) is involved in “silencing” genes so that they are not “read” by the cellular machinery that decodes genetic information, effectively keeping the genetic information in the “off” state. PRC2 silences genes by chemically depositing tri-methylation marks on histone H3 at lysine 27. Failure to regulate the activity of PRC2 not only impairs the process of development, but also contributes to the reversal of cell differentiation and the uncontrolled cell growth that are the hallmarks of cancer.
A team of scientists at Berkeley Lab and UC Berkeley have uncovered the molecular basis for the recruitment of PRC2 to certain locations of the genome and for the regulation of its activity. In a study published January 22 in Science, the researchers describe the structure of PRC2 while bound to a biologically relevant chromatin target. Using cryo-electron microscopy (cryo-EM), they uncovered crucial structural and functional information about this key regulator of cell differentiation and identity.
Eva Nogales Named a 2020 Biophysical Society Fellow
Eva Nogales, a senior faculty scientist Molecular Biophysics and Integrated Bioimaging (MBIB), has been named a 2020 Fellow of the Biophysics Society. The international scientific society was created to promote the development and dissemination of biophysics knowledge through meetings, publications, community outreach, and career placement.
Nogales, who is also a Howard Hughes Medical Institute (HHMI) investigator and professor at UC Berkeley, is recognized for her demonstrated excellence in science and contributions to the success and vitality of the biophysics field. In addition, the society cited her efforts to push cryo-EM barriers and the resulting structural insights into the central dogma machinery and cytoskeleton interactions and dynamics in cell division, and her structural studies of microtubules and associated proteins, and of machineries regulating gene expression.
The awardees will be formally honored at the 2020 Annual Biophysical Society Meeting to be held in San Diego February 15–19.
Eva Nogales Elected to European Molecular Biology Organization
The European Molecular Biology Organization (EMBO) has elected Molecular Biophysics and Integrated Bioimaging (MBIB) senior faculty scientist Eva Nogales as an associate member. The organization of more than 1,800 leading researchers promotes excellence in the life sciences in Europe and beyond. Nogales, who is also a Howard Hughes Medical Institute (HHMI) investigator and professor at UC Berkeley, is among 56 new members and associate members EMBO will formally welcome at the annual meeting in Heidelberg, Germany, in October 2019.
Working the Core: Insights into Transcription Factor IIH Function
A team of scientists from the Molecular Biophysics and Integrated Bioimaging (MBIB) Division and UC Berkeley has constructed the first complete atomic blueprint of a complicated molecular machine that is crucial to repairing and reading DNA. These protein assemblies, human transcription initiation factor IIH (TFIIH), are essential to survival, yet we know little about how they function because, until recently, it was impossible to accurately describe their structure.
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