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MNaa10-KO liver immunoprecipitation

ABSTRACT: NAA10-mediated N-terminal acetylation is widespread and has been considered essential for viability in many model organisms. However, a Naa10 null mouse model is viable and has intact global N-terminal acetylation levels. The purpose of this project was to assess the N-terminal acetyltransferase activity of NAA15 immunoprecipitates from Naa10-KO mouse liver. We show that there is a novel paralog of Naa10 present in mice, termed Naa12, with a NatA-type enzymatic activity. We demonstrate the presence of Naa12 by detecting unique Naa12 peptides in NAA15 immunoprecipitates.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Liver

SUBMITTER: Rasmus Ree

LAB HEAD: Thomas Arnesen

PROVIDER: PXD026684 | Pride | 2021-08-17

REPOSITORIES: Pride

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Naa12 compensates for Naa10 in mice in the amino-terminal acetylation pathway.

Kweon Hyae Yon HY Lee Mi-Ni MN Dorfel Max M Seo Seungwoon S Gottlieb Leah L PaPazyan Thomas T McTiernan Nina N Ree Rasmus R Bolton David D Garcia Andrew A Flory Michael M Crain Jonathan J Sebold Alison A Lyons Scott S Ismail Ahmed A Marchi Elaine E Sonn Seong-Keun SK Jeong Se-Jin SJ Jeon Sejin S Ju Shinyeong S Conway Simon J SJ Kim Taesoo T Kim Hyun-Seok HS Lee Cheolju C Roh Tae-Young TY Arnesen Thomas T Marmorstein Ronen R Oh Goo Taeg GT Lyon Gholson J GJ

eLife 20210806

Amino-terminal acetylation is catalyzed by a set of N-terminal acetyltransferases (NATs). The NatA complex (including X-linked Naa10 and Naa15) is the major acetyltransferase, with 40-50% of all mammalian proteins being potential substrates. However, the overall role of amino-terminal acetylation on a whole-organism level is poorly understood, particularly in mammals. Male mice lacking Naa10 show no globally apparent in vivo amino-terminal acetylation impairment and do not exhibit complet ...[more]

PMID: 34355692

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