Structural basis of HypK regulating N-terminal acetylation by the NatA complex

N-terminal acetylation is a common eukaryotic protein modification that is primarily catalysed by the N-acetyl transferase complex A (NatA). Here, the authors present the crystal structure of NatA bound to Huntingtin yeast two-hybrid protein K (HypK) and show that HypK is a negative regulator of Nat...

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Autores principales:	Felix Alexander Weyer, Andrea Gumiero, Karine Lapouge, Gert Bange, Jürgen Kopp, Irmgard Sinning
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/9c328f88012a4a40805c0b5463ad51b5
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spelling	oai:doaj.org-article:9c328f88012a4a40805c0b5463ad51b52021-12-02T17:06:04ZStructural basis of HypK regulating N-terminal acetylation by the NatA complex10.1038/ncomms157262041-1723https://doaj.org/article/9c328f88012a4a40805c0b5463ad51b52017-06-01T00:00:00Zhttps://doi.org/10.1038/ncomms15726https://doaj.org/toc/2041-1723N-terminal acetylation is a common eukaryotic protein modification that is primarily catalysed by the N-acetyl transferase complex A (NatA). Here, the authors present the crystal structure of NatA bound to Huntingtin yeast two-hybrid protein K (HypK) and show that HypK is a negative regulator of NatA.Felix Alexander WeyerAndrea GumieroKarine LapougeGert BangeJürgen KoppIrmgard SinningNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Felix Alexander Weyer Andrea Gumiero Karine Lapouge Gert Bange Jürgen Kopp Irmgard Sinning Structural basis of HypK regulating N-terminal acetylation by the NatA complex
description	N-terminal acetylation is a common eukaryotic protein modification that is primarily catalysed by the N-acetyl transferase complex A (NatA). Here, the authors present the crystal structure of NatA bound to Huntingtin yeast two-hybrid protein K (HypK) and show that HypK is a negative regulator of NatA.
format	article
author	Felix Alexander Weyer Andrea Gumiero Karine Lapouge Gert Bange Jürgen Kopp Irmgard Sinning
author_facet	Felix Alexander Weyer Andrea Gumiero Karine Lapouge Gert Bange Jürgen Kopp Irmgard Sinning
author_sort	Felix Alexander Weyer
title	Structural basis of HypK regulating N-terminal acetylation by the NatA complex
title_short	Structural basis of HypK regulating N-terminal acetylation by the NatA complex
title_full	Structural basis of HypK regulating N-terminal acetylation by the NatA complex
title_fullStr	Structural basis of HypK regulating N-terminal acetylation by the NatA complex
title_full_unstemmed	Structural basis of HypK regulating N-terminal acetylation by the NatA complex
title_sort	structural basis of hypk regulating n-terminal acetylation by the nata complex
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/9c328f88012a4a40805c0b5463ad51b5
work_keys_str_mv	AT felixalexanderweyer structuralbasisofhypkregulatingnterminalacetylationbythenatacomplex AT andreagumiero structuralbasisofhypkregulatingnterminalacetylationbythenatacomplex AT karinelapouge structuralbasisofhypkregulatingnterminalacetylationbythenatacomplex AT gertbange structuralbasisofhypkregulatingnterminalacetylationbythenatacomplex AT jurgenkopp structuralbasisofhypkregulatingnterminalacetylationbythenatacomplex AT irmgardsinning structuralbasisofhypkregulatingnterminalacetylationbythenatacomplex
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Structural basis of HypK regulating N-terminal acetylation by the NatA complex

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