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

Kweon, Hyae Yon, Lee, Mi-Ni, Dorfel, Max, Seo, Seungwoon, Gottlieb, Leah, PaPazyan, Thomas, McTiernan, Nina, Ree, Rasmus, Bolton, David, Garcia, Andrew, Flory, Michael, Crain, Jonathan, Sebold, Alison, Lyons, Scott, Ismail, Ahmed, Marchi, Elaine, Sonn, Seong-Keun, Jeong, Se-Jin, Jeon, Sejin, Ju, Shinyeong, Conway, Simon J, Kim, Taesoo, Kim, Hyun-Seok, Lee, Cheolju, Roh, Tae-Young, Arnesen, Thomas, Marmorstein, Ronen, Oh, Gootaeg, Lyon, Gholson J (August 2021) Naa12 compensates for Naa10 in mice in the amino-terminal acetylation pathway. eLife, 10. ISSN 2050-084X

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URL: https://pubmed.ncbi.nlm.nih.gov/34355692/
DOI: 10.7554/eLife.65952

Abstract

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 complete embryonic lethality. Rather Naa10 nulls display increased neonatal lethality, and the majority of surviving undersized mutants exhibit a combination of hydrocephaly, cardiac defects, homeotic anterior transformation, piebaldism and urogenital anomalies. Naa12 is a previously unannotated Naa10-like paralogue with NAT activity that genetically compensates for Naa10. Mice deficient for Naa12 have no apparent phenotype, whereas mice deficient for Naa10 and Naa12 display embryonic lethality. The discovery of Naa12 adds to the currently known machinery involved in amino-terminal acetylation in mice.

Item Type: Paper
Subjects: organism description > animal > developmental stage
organism description > animal > mammal > rodent > mouse
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > N-terminal acetylation
CSHL Authors:
Communities: CSHL labs > Lyons lab
SWORD Depositor: CSHL Elements
Depositing User: CSHL Elements
Date: 6 August 2021
Date Deposited: 09 Aug 2021 13:23
Last Modified: 15 Sep 2021 20:17
PMCID: PMC8376253
URI: https://repository.cshl.edu/id/eprint/40313

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