PXD015875

PXD015875 is an original dataset announced via ProteomeXchange.

Title	Global profiling of acetylation reveals a new family with dual-specific lysine and N-terminal acetyltransferase activity in the plastids of Arabidopsis
Description	Protein acetylation is a universally conserved modification occurring on N-termini (N--acetylation, NTA) and on internal lysines residues (-lysine-acetylation, KA). So far, NTA and KA were known to be supported by distinct families of enzymes (NATs and KATs, respectively), despite most of them share a common GCN5-related N-acetyltransferase (GNAT) domain. Although recent reports indicate that both NTA and KA occur frequently in plant plastids, little is known about the machinery involved in plastid acetylations and why these modifications are that frequent in this organelle. Searches for new putative NAT and KAT genes in Arabidopsis thaliana illuminate a common pool of ten putative candidates, displaying a number of unique features both at the level of conserved key residues and motifs. Here, we show that eight out of the ten candidates are associated with the plastids. In vivo investigation based on global quantitative mass spectrometry of these enzymes revealed that they exhibit a number of unique features, supporting both NAT and KAT activities of the plastids. All identified enzymes show distinct KAT substrate specificity and display unexpected relaxed NAT substrate specificity, each with differences in terms of NTA yields and preferred substrates. Together, this study reveals an unexpected multitasking protein modification machinery dedicated to the plastids of plant. We suggest that this machinery likely evolved to support specific needs of this organelle.
HostingRepository	jPOST
AnnounceDate	2020-07-07
AnnouncementXML	Submission_2023-02-07_00:03:40.286.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Jürgen Eirich
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	S-carboxamidomethyl-L-cysteine; N6-acetyl-L-lysine; L-methionine sulfoxide
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2019-10-17 07:40:52	ID requested
1	2020-07-07 06:58:55	announced
2	2021-02-04 16:42:10	announced	2021-02-04: Updated FTP location.
3	2022-09-18 03:35:11	announced	2022-09-18: Updated FTP location.
⏵ 4	2023-02-07 00:03:41	announced	2023-02-07: Updated PubMed.

Bienvenut WV, Br, ü, nje A, Boyer JB, M, ü, hlenbeck JS, Bernal G, Lassowskat I, Dian C, Linster E, Dinh TV, Koskela MM, Jung V, Seidel J, Schyrba LK, Ivanauskaite A, Eirich J, Hell R, Schwarzer D, Mulo P, Wirtz M, Meinnel T, Giglione C, Finkemeier I, Dual lysine and N-terminal acetyltransferases reveal the complexity underpinning protein acetylation. Mol Syst Biol, 16(7):e9464(2020) [pubmed]

submitter keyword: Arabidopsis Thaliana, Acetylation, Acetyltransferase, Plant, Chloroplast, Immuno Precipitation

Iris Finkemeyer
lab head
Jürgen Eirich
contact affiliation	University of Münster - WWU - Institute for Biology and Biotechnology of Plants
dataset submitter

jPOST dataset URI

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