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

In eukaryotes, N-terminal acetylation is one of the most common protein modifications involved in a wide range of biological processes. Most N-acetyltransferase complexes (NATs) act co-translationally, with the heterodimeric NatA complex modifying the majority of substrate proteins. Here we show tha...

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Hauptverfasser: Weyer, Felix Alexander (VerfasserIn) , Gumiero, Andrea (VerfasserIn) , Lapouge, Karine (VerfasserIn) , Bange, Gert (VerfasserIn) , Kopp, Jürgen (VerfasserIn) , Sinning, Irmgard (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 6 June 2017
In: Nature Communications
Year: 2017, Jahrgang: 8
ISSN:2041-1723
DOI:10.1038/ncomms15726
Online-Zugang:Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1038/ncomms15726
Verlag, kostenfrei, Volltext: https://www.nature.com/articles/ncomms15726
Volltext
Verfasserangaben:Felix Alexander Weyer, Andrea Gumiero, Karine Lapouge, Gert Bange, Jürgen Kopp & Irmgard Sinning

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520 |a In eukaryotes, N-terminal acetylation is one of the most common protein modifications involved in a wide range of biological processes. Most N-acetyltransferase complexes (NATs) act co-translationally, with the heterodimeric NatA complex modifying the majority of substrate proteins. Here we show that the Huntingtin yeast two-hybrid protein K (HypK) binds tightly to the NatA complex comprising the auxiliary subunit Naa15 and the catalytic subunit Naa10. The crystal structures of NatA bound to HypK or to a N-terminal deletion variant of HypK were determined without or with a bi-substrate analogue, respectively. The HypK C-terminal region is responsible for high-affinity interaction with the C-terminal part of Naa15. In combination with acetylation assays, the HypK N-terminal region is identified as a negative regulator of the NatA acetylation activity. Our study provides mechanistic insights into the regulation of this pivotal protein modification. 
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