Advances in cryogenic electron microscopy have enabled an international team of experts to visualize the structure of a cyanobacterial phycobilisome with nearly atomic resolution. The work, a collaboration among researchers at Michigan State University, UC Berkeley, Berkeley Lab, and the University of South Bohemia in the Czech Republic, was published in Nature. Knowing the position of different proteins and pigments helps scientist better understand this natural process and can inspire future applications in areas such as renewable energy and environmental remediation.
The American Association for the Advancement of Science (AAAS) has announced that 564 of its members—among them four scientists at Berkeley Lab—have been elected Fellows as part of the 2021 class. The two newly named Fellows from the Biosciences Area are: Eva Nogales, a senior faculty scientist in the Molecular Biophysics and Integrated Bioimaging (MBIB) Division, and Scott Baker an affiliate with the Joint BioEnergy Institute (JBEI).
A team led by Eva Nogales, senior faculty scientist in the Molecular Biophysics and Integrated Bioimaging (MBIB) Division, has produced the first detailed 3D structure of human SAGA, a 20-piece molecular machine that’s crucial to life. The structure, reported in Nature Structural & Molecular Biology, revealed some unexpected differences between the human and yeast versions of SAGA and could guide the development of drugs to treat diseases that arise when this complex malfunctions.
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.
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.