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

Hyae Yon Kweon, Mi-Ni Lee, Max Dörfel, Seungwoon Seo, Leah Gottlieb, Thomas Papazyan, Nina McTiernan, Rasmus Ree, David Bolton, Andrew Garcia, Michael Flory, Jonathan Crain, Alison Sebold, Scott Lyons, Ahmed Ismail, Elaine Marchi, Seong-keun Sonn, Se-Jin Jeong, Sejin Jeon, Shinyeong Ju, Simon J. Conway, TaeSoo Kim, Hyun-Seok Kim, View ORCID ProfileCheolju Lee, Tae-Young Roh, Thomas Arnesen, View ORCID ProfileRonen Marmorstein, Goo Taeg Oh, View ORCID ProfileGholson J. Lyon
doi: https://doi.org/10.1101/2020.12.19.422860
Hyae Yon Kweon
1Department of Life Science and College of Natural Sciences, Ewha Womans University, Seoul, Republic of Korea
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Mi-Ni Lee
1Department of Life Science and College of Natural Sciences, Ewha Womans University, Seoul, Republic of Korea
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  • For correspondence: minilee@kribb.re.kr tinymini@ewhain.net gholsonjlyon@gmail.com gholson.j.lyon@opwdd.ny.gov gootaeg@ewha.ac.kr
Max Dörfel
2Stanley Institute for Cognitive Genomics, Cold Spring Harbor Laboratory, Woodbury, New York, United States of America
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Seungwoon Seo
1Department of Life Science and College of Natural Sciences, Ewha Womans University, Seoul, Republic of Korea
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Leah Gottlieb
3Department of Chemistry, University of Pennsylvania, Philadelphia, United States of America
4Abramson Family Cancer Research Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, United States of America
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Thomas Papazyan
2Stanley Institute for Cognitive Genomics, Cold Spring Harbor Laboratory, Woodbury, New York, United States of America
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Nina McTiernan
5Department of Biomedicine, University of Bergen, Bergen, Norway
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Rasmus Ree
5Department of Biomedicine, University of Bergen, Bergen, Norway
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David Bolton
6Department of Molecular Biology, New York State Institute for Basic Research in Developmental Disabilities, Staten Island, New York, United States of America
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Andrew Garcia
7Department of Human Genetics, New York State Institute for Basic Research in Developmental Disabilities, Staten Island, New York, United States of America
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Michael Flory
8Research Design and Analysis Service, New York State Institute for Basic Research in Developmental Disabilities, Staten Island, New York, United States of America
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Jonathan Crain
2Stanley Institute for Cognitive Genomics, Cold Spring Harbor Laboratory, Woodbury, New York, United States of America
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Alison Sebold
2Stanley Institute for Cognitive Genomics, Cold Spring Harbor Laboratory, Woodbury, New York, United States of America
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Scott Lyons
2Stanley Institute for Cognitive Genomics, Cold Spring Harbor Laboratory, Woodbury, New York, United States of America
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Ahmed Ismail
2Stanley Institute for Cognitive Genomics, Cold Spring Harbor Laboratory, Woodbury, New York, United States of America
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Elaine Marchi
7Department of Human Genetics, New York State Institute for Basic Research in Developmental Disabilities, Staten Island, New York, United States of America
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Seong-keun Sonn
1Department of Life Science and College of Natural Sciences, Ewha Womans University, Seoul, Republic of Korea
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Se-Jin Jeong
9Center for Cardiovascular Research, Washington University School of Medicine, Saint Louis, Missouri, United States of America
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Sejin Jeon
1Department of Life Science and College of Natural Sciences, Ewha Womans University, Seoul, Republic of Korea
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Shinyeong Ju
10Center for Theragnosis, Korea Institute of Science and Technology, Seoul, Republic of Korea
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Simon J. Conway
11Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, United States of America
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TaeSoo Kim
1Department of Life Science and College of Natural Sciences, Ewha Womans University, Seoul, Republic of Korea
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Hyun-Seok Kim
1Department of Life Science and College of Natural Sciences, Ewha Womans University, Seoul, Republic of Korea
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Cheolju Lee
10Center for Theragnosis, Korea Institute of Science and Technology, Seoul, Republic of Korea
12Department of Converging Science and Technology, KHU-KIST, Kyung Hee University, Seoul, Republic of Korea
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  • ORCID record for Cheolju Lee
Tae-Young Roh
13Department of Life Sciences, Pohang University of Science and Technology, Pohang, Republic of Korea
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Thomas Arnesen
5Department of Biomedicine, University of Bergen, Bergen, Norway
14Department of Biological Sciences, University of Bergen, Bergen, Norway
15Department of Surgery, Haukeland University Hospital, Bergen, Norway
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Ronen Marmorstein
3Department of Chemistry, University of Pennsylvania, Philadelphia, United States of America
4Abramson Family Cancer Research Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, United States of America
16Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, United States of America
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Goo Taeg Oh
1Department of Life Science and College of Natural Sciences, Ewha Womans University, Seoul, Republic of Korea
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  • For correspondence: minilee@kribb.re.kr tinymini@ewhain.net gholsonjlyon@gmail.com gholson.j.lyon@opwdd.ny.gov gootaeg@ewha.ac.kr
Gholson J. Lyon
2Stanley Institute for Cognitive Genomics, Cold Spring Harbor Laboratory, Woodbury, New York, United States of America
7Department of Human Genetics, New York State Institute for Basic Research in Developmental Disabilities, Staten Island, New York, United States of America
17George A. Jervis Clinic, New York State Institute for Basic Research in Developmental Disabilities, Staten Island, New York, United States of America
18Biology PhD Program, The Graduate Center, The City University of New York, New York, United States of America
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  • ORCID record for Gholson J. Lyon
  • For correspondence: minilee@kribb.re.kr tinymini@ewhain.net gholsonjlyon@gmail.com gholson.j.lyon@opwdd.ny.gov gootaeg@ewha.ac.kr
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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.

Competing Interest Statement

The authors have declared no competing interest.

Footnotes

  • We added new IP-Mass spec data demonstrating specific peptides unique to mouse Naa12. We include enzymatic analysis of a complex between mouse Naa12 and human NAA15. We have also included an entirely new section of the paper, titled Genotype distribution modeling of Naa10- and Naa12-deficient offspring. We also responded to extensive peer review comments, by editing throughout the manuscript.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC 4.0 International license.
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Naa12 compensates for Naa10 in mice in the amino-terminal acetylation pathway
Hyae Yon Kweon, Mi-Ni Lee, Max Dörfel, Seungwoon Seo, Leah Gottlieb, Thomas Papazyan, Nina McTiernan, Rasmus Ree, David Bolton, Andrew Garcia, Michael Flory, Jonathan Crain, Alison Sebold, Scott Lyons, Ahmed Ismail, Elaine Marchi, Seong-keun Sonn, Se-Jin Jeong, Sejin Jeon, Shinyeong Ju, Simon J. Conway, TaeSoo Kim, Hyun-Seok Kim, Cheolju Lee, Tae-Young Roh, Thomas Arnesen, Ronen Marmorstein, Goo Taeg Oh, Gholson J. Lyon
bioRxiv 2020.12.19.422860; doi: https://doi.org/10.1101/2020.12.19.422860
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Naa12 compensates for Naa10 in mice in the amino-terminal acetylation pathway
Hyae Yon Kweon, Mi-Ni Lee, Max Dörfel, Seungwoon Seo, Leah Gottlieb, Thomas Papazyan, Nina McTiernan, Rasmus Ree, David Bolton, Andrew Garcia, Michael Flory, Jonathan Crain, Alison Sebold, Scott Lyons, Ahmed Ismail, Elaine Marchi, Seong-keun Sonn, Se-Jin Jeong, Sejin Jeon, Shinyeong Ju, Simon J. Conway, TaeSoo Kim, Hyun-Seok Kim, Cheolju Lee, Tae-Young Roh, Thomas Arnesen, Ronen Marmorstein, Goo Taeg Oh, Gholson J. Lyon
bioRxiv 2020.12.19.422860; doi: https://doi.org/10.1101/2020.12.19.422860

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