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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: | , , , , , |
| 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
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| Gesamtaufnahme: |
: Nature Communications, 8(2017) Artikel-Nummer 15726, 10 Seiten
, volume:8 |
| Quelle: | Verbunddaten SWB Lizenzfreie Online-Ressourcen |
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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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| contents | 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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| spelling | Weyer, Felix Alexander VerfasserIn (DE-588)1099734142 (DE-627)858754312 (DE-576)46935545X aut, 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, 6 June 2017, Text txt rdacontent, Computermedien c rdamedia, Online-Ressource cr rdacarrier, Gesehen am 07.09.2018, 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., Gumiero, Andrea VerfasserIn (DE-588)1166462803 (DE-627)1030437866 (DE-576)510785107 aut, Lapouge, Karine VerfasserIn (DE-588)1166462900 (DE-627)1030438048 (DE-576)510785050 aut, Bange, Gert VerfasserIn (DE-588)135801354 (DE-627)57166489X (DE-576)300653719 aut, Kopp, Jürgen 1964- VerfasserIn (DE-588)120731878 (DE-627)704953692 (DE-576)292359284 aut, Sinning, Irmgard 1960- VerfasserIn (DE-588)1027598617 (DE-627)72945133X (DE-576)166290580 aut, Enthalten in Nature Communications [London] : Nature Publishing Group UK, 2010 8(2017) Artikel-Nummer 15726, 10 Seiten Online-Ressource (DE-627)626457688 (DE-600)2553671-0 (DE-576)331555905 2041-1723 nnns, volume:8 year:2017, http://dx.doi.org/10.1038/ncomms15726 Verlag Resolving-System kostenfrei Volltext, https://www.nature.com/articles/ncomms15726 Verlag kostenfrei Volltext, http://dx.doi.org/10.1038/ncomms15726 LFER, LFER 2018-09-13T00:00:00Z |
| spellingShingle | Weyer, Felix Alexander, Gumiero, Andrea, Lapouge, Karine, Bange, Gert, Kopp, Jürgen, Sinning, Irmgard, 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 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. |
| swb_id_str | 510785190 |
| title | Structural basis of HypK regulating N-terminal acetylation by the NatA complex |
| title_auth | 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 Felix Alexander Weyer, Andrea Gumiero, Karine Lapouge, Gert Bange, Jürgen Kopp & Irmgard Sinning |
| title_fullStr | 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 |
| title_full_unstemmed | 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 |
| title_in_hierarchy | 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, |
| title_short | 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 |
| url | http://dx.doi.org/10.1038/ncomms15726, https://www.nature.com/articles/ncomms15726 |