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Structural basis of HypK regulating N-terminal acetylation by the NatA complex
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| Published in: | Nature Communications 8(2017) Artikel-Nummer 15726, 10 Seiten |
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| Authors and Corporations: | , , , , , |
| Title: | Structural basis of HypK regulating N-terminal acetylation by the NatA complex/ Felix Alexander Weyer, Andrea Gumiero, Karine Lapouge, Gert Bange, Jürgen Kopp & Irmgard Sinning |
| Type of Resource: | E-Book Component Part |
| Language: | English |
| published: |
6 June 2017
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| Series: |
: Nature Communications, 8(2017) Artikel-Nummer 15726, 10 Seiten
, volume:8 |
| Source: | Verbunddaten SWB Lizenzfreie Online-Ressourcen |
| Abstract: | 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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| Item Description: | Gesehen am 07.09.2018 |
| ISSN: |
2041-1723
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| DOI: | 10.1038/ncomms15726 |