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DTSTART:20070311T020000
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DTSTAMP:20211011T181537
DTSTART;TZID=America/Detroit:20211011T160000
DTEND;TZID=America/Detroit:20211011T173000
SUMMARY:Other:Integrative structural biology of telomerase
DESCRIPTION:Telomerase is a unique RNA-containing reverse transcriptase that synthesizes the 3’-end of\ntelomeres. It is a highly regulated determinant of tumorigenesis\, cellular aging\, and stem cell\nrenewal. All telomerases contain a catalytic core comprising telomerase reverse transcriptase\n(TERT) and telomerase RNA (TER)\, along with other proteins involved in biogenesis\, assembly\,\nand activation. TER has an integral template complementary to ~1.5 telomere repeats used by\nTERT to repetitively synthesize the telomere repeat (TTGGGG in Tetrahymena and TTAGGG in\nhuman)\, but this template alone is insufficient for activity with TERT. Our interest in telomeres\nand telomerase began in the 1990’s when we studied the structure of telomeric repeat\nsequences\, using NMR to determine the first G-quadruplex structures. For the past decade\, we\nhave been using an integrative structural biology approach combining NMR\, X-ray\ncrystallography\, and electron microscopy to study the structure and function of Tetrahymena\nand human telomerase. I will discuss how our NMR studies of telomerase RNA structure and\ndynamics\, X-ray crystal structures of protein-TER complexes\, and cryo electron microscopy of\nthe holoenzyme have together helped reveal the structure\, function\, and interactions of this\nremarkable enzyme.\nJuli Feigon (University of California)
UID:85450-21626469@events.umich.edu
URL:https://events.umich.edu/event/85450
CLASS:PUBLIC
STATUS:CONFIRMED
CATEGORIES:Biosciences,Chemistry,Science
LOCATION:Chemistry Dow Lab - 1640
CONTACT:
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