Alfred Lentzsch

Great new review on NAC from the Deuerling lab!

Check out our recent paper! Using biochemical reconstitution, computational modeling, and cellular assays, we show that the regulatory protein HYPK fine-tunes ribosome binding of the cotranslational N-acetyltransferase NatA, enabling it to acetylate ~40% of the proteome.

ZAK activation at the collided ribosome - Nature The kinase ZAK is activated at collided ribosomes to mediate the ribotoxic stress response.

Nature research paper: ZAK activation at the collided ribosome

go.nature.com/4a9cika

Mechanism of cotranslational protein N-myristoylation in human cells In structure-function studies, Gamerdinger and Echeverria et al. uncover the cotranslational mechanism of N-myristoyltransferases (NMTs), essential enzymes that attach a lipid anchor to newborn proteins. They show that NMT activity is orchestrated by a key regulator at the ribosomal tunnel exit, the nascent polypeptide-associated complex (NAC).

Online Now: Mechanism of cotranslational protein N-myristoylation in human cells Online now:

Mechanistic insights into protein biogenesis and maturation on the ribosome The ribosome is a major cellular machine that converts genetic information into biological function. Emerging data show that the ribosome is not only …

Check out this review we wrote in JMB, together with Profs. Jae Ho Lee and Shu-ou Shan, on the mechanisms of cotranslational protein biogenesis!