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DTSTART;TZID=America/Chicago:20260505T100000
DTEND;TZID=America/Chicago:20260505T110000
DTSTAMP:20260419T100838Z
SUMMARY:BMG Faculty Candidate: Alfred Lentzsch\, PhD\, Johns Hopkins
UID:641801@northwestern.edu
TZID:America/Chicago
DESCRIPTION:BMG Faculty Candidate Seminar Department of Biochemistry and Molecular Genetics presents:  "A dynamic assembly hub orchestrates cotranslational protein modification"  Alfred Lentzsch\, PhD Assistant Research Scientist Department of Molecular Biology and Genetics Johns Hopkins University School of Medicine Baltimore\, MD  Abstract:  The N-termini of eukaryotic proteins undergo a variety of chemical modifications that are essential for organismal function. While the range of modifications and substrates has been known for decades\, the biochemical mechanisms underlying their addition remain poorly understood. These modifications are installed cotranslationally on the ribosome by a collection of enzymes that must find their correct substrates within a narrow window during translation. Furthermore\, because all of these enzymes act near the polypeptide exit tunnel on the ribosome\, they must coordinate in space and time with each other during translation. Here\, I will discuss the mechanistic basis for initiator methionine excision by MetAP1\, N-terminal acetylation by NatA\, and N-terminal myristoylation by NMT1. I will show that all three enzymes are coordinated by the nascent polypeptide-associated complex (NAC) at the polypeptide exit tunnel\, establishing NAC as a dynamic assembly hub that orchestrates protein biogenesis.  Hosts: Drs. Ali Shilatifard\, Chairman\, and Issam Ben-Sahra\, Associate Professor\, Department of Biochemistry and Molecular Genetics
LOCATION:Simpson Querrey Biomedical Research Center\, Simpson Querrey Auditorium\, 303 E. Superior Street\, Chicago\, IL 60611
TRANSP:OPAQUE
URL:https://planitpurple.northwestern.edu/event/641801
CREATED:20230106T060000Z
STATUS:CONFIRMED
LAST-MODIFIED:20260417T193119Z
PRIORITY:0
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