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

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...

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Autores principales: 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, Goo Taeg, Lyon, Gholson J
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8376253/
https://www.ncbi.nlm.nih.gov/pubmed/34355692
http://dx.doi.org/10.7554/eLife.65952
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author 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, Goo Taeg
Lyon, Gholson J
author_facet 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, Goo Taeg
Lyon, Gholson J
author_sort Kweon, Hyae Yon
collection PubMed
description 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 paralog 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.
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spelling pubmed-83762532021-08-20 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, Goo Taeg Lyon, Gholson J eLife Developmental Biology 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 paralog 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. eLife Sciences Publications, Ltd 2021-08-06 /pmc/articles/PMC8376253/ /pubmed/34355692 http://dx.doi.org/10.7554/eLife.65952 Text en © 2021, Kweon et al https://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited.
spellingShingle Developmental Biology
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, Goo Taeg
Lyon, Gholson J
Naa12 compensates for Naa10 in mice in the amino-terminal acetylation pathway
title Naa12 compensates for Naa10 in mice in the amino-terminal acetylation pathway
title_full Naa12 compensates for Naa10 in mice in the amino-terminal acetylation pathway
title_fullStr Naa12 compensates for Naa10 in mice in the amino-terminal acetylation pathway
title_full_unstemmed Naa12 compensates for Naa10 in mice in the amino-terminal acetylation pathway
title_short Naa12 compensates for Naa10 in mice in the amino-terminal acetylation pathway
title_sort naa12 compensates for naa10 in mice in the amino-terminal acetylation pathway
topic Developmental Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8376253/
https://www.ncbi.nlm.nih.gov/pubmed/34355692
http://dx.doi.org/10.7554/eLife.65952
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