Proteomics

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Mass-spectrometry based quantification of HYPK, NAA10 and NAA15 protein steady-state levels in Arabidopsis thaliana mutants carrying a T-DNA insertion in the HYPK gene.

ABSTRACT: N-alpha terminal acetylation is one of the major protein modifications in eukaryotes carried out by distinct Nats (N-alpha acetyltransferases). The core NatA complex is composed of the catalytic NAA10 and the auxiliary NAA15 subunit and co-translationally acetylates majority of the cytosolic proteins. HYPK interacts with NatA core complex in human and fungus in vivo and in vitro, regulating its activity. Here, a mass spectrometry approach was applied to quantify the steady-state levels of the core NatA subunits, NAA10 and NAA15 and of HYPK in the roots of Arabidopsis mutants carrying a T-DNA insertion in the HYPK gene (AT3G06610).

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Leaf

SUBMITTER: Thomas Ruppert  

LAB HEAD: Thomas Ruppert

PROVIDER: PXD023599 | Pride | 2022-08-12

REPOSITORIES: Pride

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Publications

HYPK promotes the activity of the <i>N</i><sup>α</sup>-acetyltransferase A complex to determine proteostasis of nonAc-X<sup>2</sup>/N-degron-containing proteins.

Miklánková Pavlína P   Linster Eric E   Boyer Jean-Baptiste JB   Weidenhausen Jonas J   Mueller Johannes J   Armbruster Laura L   Lapouge Karine K   De La Torre Carolina C   Bienvenut Willy W   Sticht Carsten C   Mann Matthias M   Meinnel Thierry T   Sinning Irmgard I   Giglione Carmela C   Hell Rüdiger R   Wirtz Markus M  

Science advances 20220615 24

In humans, the Huntingtin yeast partner K (HYPK) binds to the ribosome-associated <i>N</i><sup>α</sup>-acetyltransferase A (NatA) complex that acetylates ~40% of the proteome in humans and <i>Arabidopsis thaliana</i>. However, the relevance of <i>Hs</i>HYPK for determining the human N-acetylome is unclear. Here, we identify the <i>At</i>HYPK protein as the first in vivo regulator of NatA activity in plants<i>. At</i>HYPK physically interacts with the ribosome-anchoring subunit of NatA and promot  ...[more]

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