Molecular mechanism of N-terminal acetylation by the ternary NatC complex.
Sign Up to like & getrecommendations! Published in 2021 at "Structure"
DOI: 10.1016/j.str.2021.05.003
Abstract: Protein N-terminal acetylation is predominantly a ribosome-associated modification, with NatA-E serving as the major enzymes. NatC is the most unusual of these enzymes, containing one Naa30 catalytic subunit and two auxiliary subunits, Naa35 and Naa38;… read more here.
Keywords: mechanism terminal; acetylation; terminal acetylation; natc complex ... See more keywords
Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates
Sign Up to like & getrecommendations! Published in 2020 at "Nature Communications"
DOI: 10.1038/s41467-020-19321-8
Abstract: The heterotrimeric NatC complex, comprising the catalytic Naa30 and the two auxiliary subunits Naa35 and Naa38, co-translationally acetylates the N-termini of numerous eukaryotic target proteins. Despite its unique subunit composition, its essential role for many… read more here.
Keywords: heterotrimeric natc; acetylation; cognate substrates; natc complex ... See more keywords