PXD006097

PXD006097 is an original dataset announced via ProteomeXchange.

Title	Identification of thioredoxin targets in Chlamydomonas reinhardtii using an affinity purification approach
Description	Thiol-based redox post-translational modifications have emerged as important mechanisms of signaling and regulation in all organisms. In this context, the small ubiquitous oxido-reductase thioredoxin plays a key role by controlling the thiol-disulfide status of target proteins. Recent redox proteomic studies revealed hundreds of proteins regulated by glutathionylation and nitrosylation in the unicellular green alga Chlamydomonas reinhardtii while much less is known about the thioredoxin interactome in this photosynthetic model organism. Using an affinity purification strategy, we identified 980 thioredoxin targets. They participate in a wide variety of metabolic pathways and cellular processes. This study broadens not only the redox regulation to new enzymes involved in metabolic pathways already known to be regulated by thioredoxins (carbon, lipid and energy metabolism) but also shed light on cellular processes for which data supporting a putative redox regulation in these processes are scarce (aromatic amino-acid biosynthesis, nuclear transport,…).
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:08:20.115.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Christophe H. MARCHAND
SpeciesList	scientific name: Chlamydomonas reinhardtii; NCBI TaxID: 3055;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue; deamidated residue
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2017-03-15 02:04:05	ID requested
1	2017-07-28 08:39:19	announced
⏵ 2	2024-10-22 04:08:20	announced	2024-10-22: Updated project metadata.

10.1016/j.molp.2017.07.009;

P, é, rez-P, é, rez ME, Mauri, è, s A, Maes A, Tourasse NJ, Hamon M, Lemaire SD, Marchand CH, The Deep Thioredoxome in Chlamydomonas reinhardtii: New Insights into Redox Regulation. Mol Plant, 10(8):1107-1125(2017) [pubmed]

curator keyword: Biological

submitter keyword: Chlamydomonas reinhardtii, redox proteomics, disulfide bonds, thioredoxin targets, redox regulation

Stéphane Lemaire
contact affiliation	Institut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Universités, UPMC Univ Paris 06, 13 rue Pierre et Marie Curie, 75005 Paris
contact email	stephane.lemaire@ibpc.fr
lab head
Christophe H. MARCHAND
contact affiliation	Institut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Universités, UPMC Univ Paris 06, 13 rue Pierre et Marie Curie, 75005 Paris
contact email	christophe.marchand@ibpc.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/2017/07/PXD006097

PRIDE project URI

• PRIDE
  1. PXD006097
     1. Label: PRIDE project
     2. Name: Identification of thioredoxin targets in Chlamydomonas reinhardtii using an affinity purification approach