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

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Veröffentlicht in: Nature Communications 8(2017) Artikel-Nummer 15726, 10 Seiten
Personen und Körperschaften: Weyer, Felix Alexander (VerfasserIn), Gumiero, Andrea (VerfasserIn), Lapouge, Karine (VerfasserIn), Bange, Gert (VerfasserIn), Kopp, Jürgen (VerfasserIn), Sinning, Irmgard (VerfasserIn)
Titel: 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
Format: E-Book-Kapitel
Sprache: Englisch
veröffentlicht:
6 June 2017
Gesamtaufnahme: : Nature Communications, 8(2017) Artikel-Nummer 15726, 10 Seiten
, volume:8
Quelle: Verbunddaten SWB
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Zusammenfassung: 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.
Beschreibung: Gesehen am 07.09.2018
ISSN: 2041-1723
DOI: 10.1038/ncomms15726