A novel human NatA Nα-terminal acetyltransferase complex: hNaa16p-hNaa10p (hNat2-hArd1) |
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| Authors: | Thomas Arnesen Darina Gromyko Diane Kagabo Matthew J Betts Kristian K Starheim Jan Erik Varhaug Dave Anderson Johan R Lillehaug |
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| Institution: | (1) Department of Molecular Biology, University of Bergen, N-5020 Bergen, Norway;(2) Department of Surgical Sciences, University of Bergen, N-5020 Bergen, Norway;(3) Department of Surgery, Haukeland University Hospital, N-5021 Bergen, Norway;(4) EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany;(5) Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229, USA;(6) Catalyst Biosciences, South San Francisco, CA 94080, USA |
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| Abstract: | Background Protein acetylation is among the most common protein modifications. The two major types are post-translational Nε-lysine acetylation catalyzed by KATs (Lysine acetyltransferases, previously named HATs (histone acetyltransferases) and co-translational
Nα-terminal acetylation catalyzed by NATs (N-terminal acetyltransferases). The major NAT complex in yeast, NatA, is composed
of the catalytic subunit Naa10p (N alpha acetyltransferase 10 protein) (Ard1p) and the auxiliary subunit Naa15p (Nat1p). The NatA complex potentially acetylates Ser-, Ala-, Thr-, Gly-,
Val- and Cys- N-termini after Met-cleavage. In humans, the homologues hNaa15p (hNat1) and hNaa10p (hArd1) were demonstrated
to form a stable ribosome associated NAT complex acetylating NatA type N-termini in vitro and in vivo. |
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