PXD009929-1

PXD009929 is an original dataset announced via ProteomeXchange.

Title	HCN regulates cellular processes through posttranslational modification of proteins by S-cyanylation
Description	Hydrogen cyanide (HCN) is coproduced with ethylene in plant cells and primarily enzymatically detoxified by the mitochondrial ß-cyanoalanine synthase (CAS-C1). Permanent or transient depletion of CAS-C1 activity in Arabidopsis results in physiological alterations in the plant that suggest that the function of HCN is a gasotransmitter molecule. Label-free quantitative proteomic analysis of enriched mitochondrial samples isolated from the wild type and cas-c1 mutant revealed significant changes in protein content, identifying 451 proteins that are absent or less abundant in cas-c1 and 353 proteins that are only present or more abundant in the mutant background. Gene ontology classification of these proteins highlights proteomic changes that explains the root hairless phenotype and the altered immune response observed in the cas-c1 mutant. The mechanism of action of cyanide as a signaling molecule has been addressed using two proteomic approaches focused on identifying the S-cyanylation of cysteine as a posttranslational modification of proteins. Both the 2-imino-thiazolidine chemical method and the direct untargeted analysis of proteins using LC-MS/MS identified a set of 163 proteins susceptible to S-cyanylation that included sedoheptulose 1, 7-bisphosphatase (SBPase), the peptidyl-prolyl cis-trans isomerase (CYP20-3) and enolase 2 (ENO2). In vitro analysis of these proteins identified that this modification in the SBPase Cys74, CYP20-3 Cys259 and ENO2 Cys346 residues affected the enzymatic activity of the enzymes. GO classification and protein-protein interaction cluster analysis revealed the function of S-cyanylation in the regulation of primary metabolic pathways, such as glycolysis, and the Calvin and S-adenosylmethionine cycles.
HostingRepository	PRIDE
AnnounceDate	2019-01-09
AnnouncementXML	Submission_2019-01-09_02:55:44.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Luis C. Romero
SpeciesList	scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702;
ModificationList	S-cyano-L-cysteine; iodoacetamide derivatized residue
Instrument	TripleTOF 5600

Revision	Datetime	Status	ChangeLog Entry
0	2018-05-28 02:12:04	ID requested
⏵ 1	2019-01-09 02:55:45	announced
2	2024-10-22 04:06:27	announced	2024-10-22: Updated project metadata.

Garc, í, a I, Arenas-Alfonseca L, Moreno I, Gotor C, Romero LC, cyanylation. Plant Physiol, 179(1):107-123(2019) [pubmed]

curator keyword: Biological

submitter keyword: Arabidopsis - root tissue - posttranslational modification - cyanylation

Luis C Romero
contact affiliation	Instituto de Bioquimica Vegetal y Fotosintesis Consejo Superior de Investigaciones Cientificas Avda. Americo Vespucio, 49 Sevilla Spain
contact email	lromero@ibvf.csic.es
lab head
Luis C. Romero
contact affiliation	Instituto Bioquimica Vegetal y Fotosintesis-CSIC
contact email	lromero@ibvf.csic.es
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/2019/01/PXD009929

PRIDE project URI

• PRIDE
  1. PXD009929
     1. Label: PRIDE project
     2. Name: HCN regulates cellular processes through posttranslational modification of proteins by S-cyanylation