HYPK promotes the activity of the Nα-acetyltransferase A complex to determine TOU

HYPK promotes the activity of the Nα-acetyltransferase A complex to determine
 TOU

HYPK promotes the activity of the Nα-acetyltransferase A complex to determine

Abstract

In humans, the Huntingtin yeast partner K (HYPK) binds to the ribosome-associated

N



-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



-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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