PXD007625

PXD007625 is an original dataset announced via ProteomeXchange.

Title	Lysine acetylation of chloroplast proteins
Description	In photosynthesis, light is absorbed by the thylakoid embedded light harvesting pigment protein complexes (LHCs) that surround the photosynthetic reaction centers, photosystem II (PSII) and photosystem I (PSI). The distribution of light energy between the photosystems is balanced through state transitions1,2, which refer to the phosphorylation-dependent association of the loosely bound (L) LHCII antenna trimer either to PSII or PSI 3,4. Apart from phosphorylation, other mechanisms regulating state transitions have not been reported this far. In this study we demonstrate that lysine (Lys) acetylation of chloroplast proteins is a prerequisite for state transitions in Arabidopsis thaliana. Knock-out mutants lacking a chloroplast acetyltransferase NSI (At1g32070; AtNSI, SNAT) show selective decreases in the Lys acetylation status of several photosynthetic proteins including PSI, PSII and LHCII subunits. Fluorescence measurements revealed that changes in the wavelength of illumination do not cause state transitions in the nsi mutants even though their LHCII phosphorylation status is not defected. Furthermore, biochemical analyses of thylakoid proteins and protein complexes showed that nsi plants are not able to accumulate the phosphorylation dependent PSI-LHCII megacomplex. Our results manifest that Lys acetylation by NSI has an integral role in the regulation of state transitions in Arabidopsis.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:40:23.611.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Ines Lassowskat
SpeciesList	scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702;
ModificationList	monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2017-09-01 04:23:28	ID requested
1	2018-07-03 06:27:12	announced
2	2018-07-30 01:26:54	announced	Updated publication reference for PubMed record(s): 29967049.
⏵ 3	2024-10-22 04:40:24	announced	2024-10-22: Updated project metadata.

10.1105/tpc.18.00155;

Koskela MM, Br, ü, nje A, Ivanauskaite A, Grabsztunowicz M, Lassowskat I, Neumann U, Dinh TV, Sindlinger J, Schwarzer D, Wirtz M, Tyystj, ä, rvi E, Finkemeier I, Mulo P, . Plant Cell, 30(8):1695-1709(2018) [pubmed]

curator keyword: Biological

submitter keyword: lysine, Arabidopsis, acetylation, chloroplast

Iris Finkemeier
contact affiliation	WWU - Westfälische Wilhelms-Universität Münster Institut für Biologie und Biotechnologie der Pflanzen Pflanzenphysiologie - AG Finkemeier Schlossplatz 7 48149 Münster
contact email	iris.finkemeier@exchange.wwu.de
lab head
Ines Lassowskat
contact affiliation	WWU Münster
contact email	ilasso@uni-muenster.de
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/2018/07/PXD007625

PRIDE project URI

• PRIDE
  1. PXD007625
     1. Label: PRIDE project
     2. Name: Lysine acetylation of chloroplast proteins