PXD001947

PXD001947 is an original dataset announced via ProteomeXchange.

Title	Identification and characterization of the first Nα-acetyltransferase in plastids
Description	Protein Nα-terminal acetylation represents one of the most abundant protein modifications of higher eukaryotes. In humans, six Nα-acetyltransferases (Nats) are responsible for the acetylation of approximately 80% of the cytosolic proteins. N-terminal protein acetylation has not been evidenced in organelles of metazoans, but in higher plants, it is a widespread modification not only in the cytosol but also in the chloroplast. In this study, we identify and characterize the first organellar-localized Nat in eukaryotes. A primary sequence-based search in Arabidopsis thaliana revealed seven putatively plastid-localized Nats of which AT2G39000 (AtNAA70) showed the highest conservation of the acetyl-CoA binding pocket. The chloroplastic localization of AtNAA70 was demonstrated by transient expression of AtNAA70:YFP in Arabidopsis mesophyll protoplasts. Homology modeling uncovered a significant conservation of tertiary structural elements between human HsNAA50 and AtNAA70. The in vivo acetylation activity of AtNAA70 was demonstrated on a number of distinct protein N alpha-termini with a newly established Nat-activity global profiling after expression of AtNAA70 in E. coli. AtNAA70 predominately acetylated proteins starting with M, A, S, and T, providing an explanation for most protein N-termini acetylation events found in chloroplasts.
HostingRepository	PRIDE
AnnounceDate	2015-06-29
AnnouncementXML	Submission_2015-06-29_05:09:18.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Willy Bienvenut
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	acetate labeling reagent (N-term) (heavy form: +3amu)
Instrument	LTQ Orbitrap

Revision	Datetime	Status	ChangeLog Entry
0	2015-03-18 02:27:24	ID requested
⏵ 1	2015-06-29 05:09:19	announced

Dinh TV, Bienvenut WV, Linster E, Feldman-Salit A, Jung VA, Meinnel T, Hell R, Giglione C, Wirtz M, -acetyltransferase in plastids by global acetylome profiling. Proteomics, 15(14):2426-35(2015) [pubmed]

curator keyword: Biological

submitter keyword: Arabidopsis thaliana, chloroplast, AtNAA70, Nα-acetyltransferase

Willy V Bienvenut
contact affiliation	Institute of Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Bâtiment 23A, 1 avenue de la Terrasse, F-91198 Gif-sur-Yvette cedex, France.
contact email	willy.bienvenut@isv.cnrs-gif.fr
lab head
Willy Bienvenut
contact affiliation	CNRS
contact email	willy.bienvenut@isv.cnrs-gif.fr
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2015/06/PXD001947

PRIDE project URI

• PRIDE
  1. PXD001947
     1. Label: PRIDE project
     2. Name: Identification and characterization of the first Nα-acetyltransferase in plastids