Dataset Information

The state transition acetyltransferase GNAT2 interacts with GNAT1 and GNAT3 in independent complexes

ABSTRACT: The acetylation of amino groups within proteins is one of the major posttranslational modifications (PTMs) in all organisms. N-terminal acetyltransferases (NATs) or lysine acetyltransferases (KATs) catalyze the transfer of the acetyl group from the donor substrate acetyl coenzyme A (Ac-CoA) to the targeted amino group, which is either the α-amino groups of N-termini or the ε-amino group of internal lysine residues. In contrast to N-terminal acetylation (NTA), the acetylation of lysine residues (KA) is reversible, whereby lysine deacetylases (KDACs) are responsible for the removal of acetyl groups from proteins. Furthermore, KA occurs posttranslationally, whereas NTA is described mainly as a cotranslational modification with the exception for N-terminally processed proteins, which are imported to chloroplasts and mitochondria

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

SUBMITTER: Iris Finkemeier

PROVIDER: PXD044167 | JPOST Repository | Mon Aug 19 00:00:00 BST 2024

REPOSITORIES: jPOST

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Dataset's files

Source:

			Action	DRS
	190417_C19_008_QHF1_PTM_Rev01_%2319_016_ABR45_K1.raw	Raw
	190417_C19_008_QHF1_PTM_Rev01_%2319_016_ABR45_K2.raw	Raw
	190417_C19_008_QHF1_PTM_Rev01_%2319_016_ABR45_K3.raw	Raw
	190417_C19_008_QHF1_PTM_Rev01_%2319_016_ABR46_K1.raw	Raw
	190417_C19_008_QHF1_PTM_Rev01_%2319_016_ABR46_K2.raw	Raw

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Publications

The Plastidial Protein Acetyltransferase GNAT1 Forms a Complex With GNAT2, yet Their Interaction Is Dispensable for State Transitions.

Brünje Annika A Füßl Magdalena M Eirich Jürgen J Boyer Jean-Baptiste JB Heinkow Paulina P Neumann Ulla U Konert Minna M Ivanauskaite Aiste A Seidel Julian J Ozawa Shin-Ichiro SI Sakamoto Wataru W Meinnel Thierry T Schwarzer Dirk D Mulo Paula P Giglione Carmela C Finkemeier Iris I

Molecular & cellular proteomics : MCP 20240928 11

Protein N-acetylation is one of the most abundant co- and post-translational modifications in eukaryotes, extending its occurrence to chloroplasts within vascular plants. Recently, a novel plastidial enzyme family comprising eight acetyltransferases that exhibit dual lysine and N-terminus acetylation activities was unveiled in Arabidopsis. Among these, GNAT1, GNAT2, and GNAT3 reveal notable phylogenetic proximity, forming a subgroup termed NAA90. Our study focused on characterizing GNAT1, closel ...[more]

PMID: 39349166

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