Biochemistry, Biophysics and Structural Biology

BBSFaculty of the Division of Biochemistry, Biophysics and Structural Biology (BBS) are engaged in advanced study of the biological chemistry of cellular metabolites; enzymatic catalysis; the structure and function of biological macromolecules, especially nucleic acids and proteins; the supramolecular organization of complex cellular assemblies, including the transcription and DNA replication proteins, biological membranes; and, regulation of biological processes such as chromosomal folding, protein secretion and intracellular signaling. These problems are being investigated in systems that range from bacteria and bacteriophage to yeast to human cells and their viruses. Faculty of this division also participate in interdepartmental programs in structural biology, chemical biology, microbiology and toxicology. Facilities include those for protein-sequence analysis, peptide and oligonucleotide synthesis, access to the synchrotron at Lawrence Berkeley National Lab for X-ray crystallography, and NMR spectrometry. 

A selection of papers published by MCB graduate students in BBS labs:

Bashore C, Dambacher CM, Goodall EA, Matyskiela ME, Lander GC, et al. (2015) Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome. Nature structural & molecular biology. 22(9):712-9.

Chen JS, Ma E, Harrington LB, Da Costa M, Tian X, Palefsky JM, Doudna JA. (2018) CRISPR-Cas12a target binding unleashes indiscriminate single-stranded DNase activity. Science.

Gonzaelz TL, Liang Y, Nguyen BN, Staskawicz BJ, Loqué D, et al. (2015) Tight regulation of plant immune responses by combining promoter and suicide exon elements. Nucleic acids research. 43(14):7152-61

Hochstrasser ML, Doudna JA. (2015) Cutting it close: CRISPR-associated endoribonuclease structure and function. Trends Biochem Sci.40(1):58-66.

Kline BC, McKay SL, Tang WW, Portnoy DA. (2015) The Listeria monocytogenes hibernation-promoting factor is required for the formation of 100S ribosomes, optimal fitness, and pathogenesis. J Bacteriol.197(3):581

Koulechova DA, Tripp KW, Hoerner G, Marquesee S. (2015) When the Scaffold Cannot Be Ignored: The Role of the Hydrophobic Core in Ligand Binding and Specificity. J Mol Biol. 427(20):3316-26-91.

Nuñez JK, Harrington LB, Kranzusch PJ, Engelman AN, Doudna JA. (2015) Foreign DNA capture during CRISPR-Cas adaptive immunity. Nature. 527(7579):535-8.

Visperas PR, Winger JA, Horton TM, Shah NH, Aum DJ, et al. (2015) Modification by covalent reaction or oxidation of cysteine residues in the tandem-SH2 domains of ZAP-70 and Syk can block phosphopeptide binding. The Biochemical journal. 401(2):310-23.

Vogan JM, Collins K. (2015) Dynamics of Human Telomerase Holoenzyme Assembly and Subunit Exchange across the Cell Cycle. The Journal of biological chemistry.290(35):21320-35.

Wright AV, Nuñez JK, Doudna J. (2015) Biology and Applications of CRISPR Systems: Harnessing Nature's Toolbox for Genome Engineering. Cell. 164(1-2):29-44.

Wright AV, Sternburg SH, Taylor DW, Staahl BT, Bardales JA, Kornfeld JE, Doudna JA. (2015) Rational design of a split-Cas9 enzyme complex. Proc Natl Acad Sci. 112(10):2984-9.

Wu RA, Dagdas YS, Yilmaz ST, Yildaz A, Collins K. (2015) Single-molecule imaging of telomerase reverse transcriptase in human telomerase holoenzyme and minimal RNP complexes. eLife. 4.

Zhang ET, He Y, Grob P, Fong YW, Nogales E, Tijan R. (2015) Architecture of the human XPC DNA repair and stem cell coactivator complex . Proc Natl Acad Sci U S A. 112(48):14817-22.