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

Author

Listed:
  • Felix Alexander Weyer

    (Heidelberg University Biochemistry Center (BZH), INF328)

  • Andrea Gumiero

    (Heidelberg University Biochemistry Center (BZH), INF328
    Present address(es): Istituto Poligrafico e Zecca dello Stato S.p.A., Via Salaria, I–712–00138 Roma, Italy (A.G.); LOEWE Center for synthetic Microbiology Philipps-University-Marburg, 35043 Marburg, Germany (G.B.))

  • Karine Lapouge

    (Heidelberg University Biochemistry Center (BZH), INF328)

  • Gert Bange

    (Heidelberg University Biochemistry Center (BZH), INF328
    Present address(es): Istituto Poligrafico e Zecca dello Stato S.p.A., Via Salaria, I–712–00138 Roma, Italy (A.G.); LOEWE Center for synthetic Microbiology Philipps-University-Marburg, 35043 Marburg, Germany (G.B.))

  • Jürgen Kopp

    (Heidelberg University Biochemistry Center (BZH), INF328)

  • Irmgard Sinning

    (Heidelberg University Biochemistry Center (BZH), INF328)

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.

Suggested Citation

  • Felix Alexander Weyer & Andrea Gumiero & Karine Lapouge & Gert Bange & Jürgen Kopp & Irmgard Sinning, 2017. "Structural basis of HypK regulating N-terminal acetylation by the NatA complex," Nature Communications, Nature, vol. 8(1), pages 1-10, August.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15726
    DOI: 10.1038/ncomms15726
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    Cited by:

    1. Marius Klein & Klemens Wild & Irmgard Sinning, 2024. "Multi-protein assemblies orchestrate co-translational enzymatic processing on the human ribosome," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    2. Eric Linster & Francy L. Forero Ruiz & Pavlina Miklankova & Thomas Ruppert & Johannes Mueller & Laura Armbruster & Xiaodi Gong & Giovanna Serino & Matthias Mann & Rüdiger Hell & Markus Wirtz, 2022. "Cotranslational N-degron masking by acetylation promotes proteome stability in plants," Nature Communications, Nature, vol. 13(1), pages 1-12, December.

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