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Spotlight on protein N-terminal acetylation

N-terminal acetylation (Nt-acetylation) is a widespread protein modification among eukaryotes and prokaryotes alike. By appending an acetyl group to the N-terminal amino group, the charge, hydrophobicity, and size of the N-terminus is altered in an irreversible manner. This alteration has implicatio...

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Detalles Bibliográficos
Autores principales: Ree, Rasmus, Varland, Sylvia, Arnesen, Thomas
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6063853/
https://www.ncbi.nlm.nih.gov/pubmed/30054468
http://dx.doi.org/10.1038/s12276-018-0116-z
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author Ree, Rasmus
Varland, Sylvia
Arnesen, Thomas
author_facet Ree, Rasmus
Varland, Sylvia
Arnesen, Thomas
author_sort Ree, Rasmus
collection PubMed
description N-terminal acetylation (Nt-acetylation) is a widespread protein modification among eukaryotes and prokaryotes alike. By appending an acetyl group to the N-terminal amino group, the charge, hydrophobicity, and size of the N-terminus is altered in an irreversible manner. This alteration has implications for the lifespan, folding characteristics and binding properties of the acetylated protein. The enzymatic machinery responsible for Nt-acetylation has been largely described, but significant knowledge gaps remain. In this review, we provide an overview of eukaryotic N-terminal acetyltransferases (NATs) and the impact of Nt-acetylation. We also discuss other functions of known NATs and outline methods for studying Nt-acetylation.
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spelling pubmed-60638532018-08-08 Spotlight on protein N-terminal acetylation Ree, Rasmus Varland, Sylvia Arnesen, Thomas Exp Mol Med Review Article N-terminal acetylation (Nt-acetylation) is a widespread protein modification among eukaryotes and prokaryotes alike. By appending an acetyl group to the N-terminal amino group, the charge, hydrophobicity, and size of the N-terminus is altered in an irreversible manner. This alteration has implications for the lifespan, folding characteristics and binding properties of the acetylated protein. The enzymatic machinery responsible for Nt-acetylation has been largely described, but significant knowledge gaps remain. In this review, we provide an overview of eukaryotic N-terminal acetyltransferases (NATs) and the impact of Nt-acetylation. We also discuss other functions of known NATs and outline methods for studying Nt-acetylation. Nature Publishing Group UK 2018-07-27 /pmc/articles/PMC6063853/ /pubmed/30054468 http://dx.doi.org/10.1038/s12276-018-0116-z Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Review Article
Ree, Rasmus
Varland, Sylvia
Arnesen, Thomas
Spotlight on protein N-terminal acetylation
title Spotlight on protein N-terminal acetylation
title_full Spotlight on protein N-terminal acetylation
title_fullStr Spotlight on protein N-terminal acetylation
title_full_unstemmed Spotlight on protein N-terminal acetylation
title_short Spotlight on protein N-terminal acetylation
title_sort spotlight on protein n-terminal acetylation
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6063853/
https://www.ncbi.nlm.nih.gov/pubmed/30054468
http://dx.doi.org/10.1038/s12276-018-0116-z
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