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BESE Special Lecture - Professor John Tainer

Start Date: April 12, 2017
End Date: April 12, 2017

​​​TITLE: The rise of DNA repair machines: novel insights and cancer implications  
DATE: Wednesday, April 12, 2017
TIME: 12:00 - 1:00 p.m.
LOCATION: Lecture Hall Level 0 · between Buildings 2 & 3

DNA damage outcomes depend upon the efficiency and fidelity of DNA damage responses (DDRs). As such, DDRs represent tightly regulated prototypical systems for linking nanoscale biomolecular structure and assembly to the biology of genomic regulation and cell signaling. I will discuss results with concepts and strategies for combining structural and imaging techniques to bridge sequence-level structural biochemistry to quantitative biological outcomes visualized in cells. I will focus on three key DDR responses: XP helicase and nucleases in bulky lesion repair, PARP/PARG/AIF damage signaling in DNA single-strand break repair, and DNA complexes in double-strand break repair. These bottom up mechanistic approaches are providing foundational knowledge to control and optimize DNA damage outcomes for synthetic lethality and for immune activation with insights for biology and cancer interventions.
John Tainer has studied biologically-interrelated stress responses for reactive oxygen, immune activation, pathogenicity, ionizing radiation, and DNA damage for >25 years. He graduated cum laude in Zoology and Anthropology from Duke’s Trinity College, and obtained his Ph.D. at Duke in David and Jane Richardson’s laboratory. He joined Scripps as a Damon Runyon Fellow in Arthur Olson’s laboratory to work on computational tools for macromolecular structures. He then joined the Scripps faculty and rose to Full Professor. At Scripps, he pioneered structures for reactive oxygen signals and regulation by superoxide dismutases, catalase, and nitric oxide synthases. He defined the first full-length structures for the membrane and fiber-forming pilin proteins and the pilus assembly for adherence and mobility. He examined mobility in antibody interactions and developed computational algorithms for measuring flexibility, intermolecular interactions and protein surface topography. At LBL he developed and directs SIBYLS, the world’s only dual-endstation synchrotron beamline for small angle x-ray scattering (SAXS) and macromolecular x-ray crystallography (MX), to determine accurate macromolecular structures, conformations and assemblies in solution and at high resolution (http://bl1231.als.lbl.gov). He solved and deposited >300 structures in the Protein Data Bank and authored >100 scientific publications cited >95 times. He defined a novel SAXS invariant, and introduced equations for objective X-ray analyses of macromolecular flexibility, mass, and similarity. At MD Anderson he focuses on DNA break and lesion repair complexes that interface repair with replication, transcription, apoptosis, and immune responses. He is the Robert A. Welch Distinguished Chair in Chemistry, Director of structural biology and Director of the National Cancer Institute’s Structural Biology of DNA Repair Program. Motivated by observations that infectious disease and radiotherapy abscopal effects can promote cancer cures, he is integrating structural and imaging technologies to dissect multi-functionality and enable mechanistic control of stress responses for biology and medicine.