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
Linda Jackson
Email