HYPK promotes the activity of the N-alpha acetyltransferase A complex to determine proteostasis of nonAc-X 2 /N-degron-containing proteins - Archive ouverte HAL
Article Dans Une Revue Science Advances Année : 2022

HYPK promotes the activity of the N-alpha acetyltransferase A complex to determine proteostasis of nonAc-X 2 /N-degron-containing proteins

Résumé

In humans, the Huntingtin yeast partner K (HYPK) binds to the ribosome-associated N α -acetyltransferase A (NatA) complex that acetylates ~40% of the proteome in humans and Arabidopsis thaliana . However, the relevance of Hs HYPK for determining the human N-acetylome is unclear. Here, we identify the At HYPK protein as the first in vivo regulator of NatA activity in plants . At HYPK physically interacts with the ribosome-anchoring subunit of NatA and promotes N α -terminal acetylation of diverse NatA substrates. Loss-of- At HYPK mutants are remarkably resistant to drought stress and strongly resemble the phenotype of NatA-depleted plants. The ectopic expression of Hs HYPK rescues this phenotype. Combined transcriptomics, proteomics, and N-terminomics unravel that HYPK impairs plant metabolism and development, predominantly by regulating NatA activity. We demonstrate that HYPK is a critical regulator of global proteostasis by facilitating masking of the recently identified nonAc-X 2 /N-degron. This N-degron targets many nonacetylated NatA substrates for degradation by the ubiquitin-proteasome system.
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hal-03754967 , version 1 (20-08-2022)

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Pavlína Miklánková, Eric Linster, Jean-Baptiste Boyer, Jonas Weidenhausen, Johannes Mueller, et al.. HYPK promotes the activity of the N-alpha acetyltransferase A complex to determine proteostasis of nonAc-X 2 /N-degron-containing proteins. Science Advances , 2022, 8 (24), pp.eabn6153. ⟨10.1126/sciadv.abn6153⟩. ⟨hal-03754967⟩
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