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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| Main Authors: | , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
6 June 2017
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| In: |
Nature Communications
Year: 2017, Volume: 8 |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/ncomms15726 |
| Online Access: | Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1038/ncomms15726 Verlag, kostenfrei, Volltext: https://www.nature.com/articles/ncomms15726 
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| Author Notes: | Felix Alexander Weyer, Andrea Gumiero, Karine Lapouge, Gert Bange, Jürgen Kopp & Irmgard Sinning |
| Summary: | 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 |
| Physical Description: | Online Resource |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/ncomms15726 |