Proteomics

Dataset Information

0

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

Dataset's files

Source:
Action DRS
180622_mus-musculus-sp_MQ_addedNAA12.fasta Fasta
MaxQuant_1.6.17.0.zip Other
Naa10KO-Ctrl-1.raw Raw
Naa10KO-Ctrl-2.raw Raw
Naa10KO-NAA15-1.raw Raw
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Publications


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 <i>Naa10</i> show no globally apparent in vivo amino-terminal acetylation impairment and do not exhibit complet  ...[more]

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