PXD010945

PXD010945 is an original dataset announced via ProteomeXchange.

Title	Proteases Shape the Chlamydomonas Secretome: Comparison to Classical Neuropeptide Processing Machinery
Description	The recent identification of catalytically active peptidylglycine -amidating monooxygenase (PAM) in Chlamydomonas reinhardtii, a unicellular green alga, suggested the presence of a PAM-like gene and peptidergic signaling in the last eukaryotic common ancestor (LECA). Homologs of prototypical neuropeptide precursors and essential peptide processing enzymes (subtilisin-like prohormone convertases and carboxypeptidase B-like enzymes) were identified in the C. reinhardtii genome. Reasoning that sexual reproduction by C. reinhardtii requires extensive communication between cells, we used mass spectroscopy to identify proteins recovered from the soluble secretome of mating gametes and searched for evidence that the putative peptidergic processing enzymes were functional.After fractionation by SDS-PAGE, signal peptide-containing proteins that remained intact or were subjected to cleavage were identified. The C. reinhardtii mating secretome contained multiple matrix metalloproteinases, cysteine endopeptidases and serine carboxypeptidases, along with one subtilisin-like proteinase. Published transcriptomic studies support a role for these proteases in sexual reproduction. Multiple extracellular matrix proteins (ECM) were identified in the soluble mating secretome. Several pherophorins, ECM glycoproteins homologous to the Volvox sex-inducing pheromone, were present; most contained typical peptide processing sites and had been cleaved, generating stable N- or C-terminal fragments. Our data suggest that subtilisin endoproteases and matrix metalloproteinases similar to those important in vertebrate peptidergic and growth factor signaling play an important role in stage transitions during the life cycle of C. reinhardtii.
HostingRepository	PRIDE
AnnounceDate	2019-07-30
AnnouncementXML	Submission_2019-07-30_05:27:07.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Navin Rauniyar
SpeciesList	scientific name: Chlamydomonas reinhardtii; NCBI TaxID: 3055;
ModificationList	amidated residue
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2018-08-30 06:19:01	ID requested
⏵ 1	2019-07-30 05:27:08	announced

Luxmi R, Blaby-Haas C, Kumar D, Rauniyar N, King SM, Mains RE, Eipper BA, Secretome: Comparison to Classical Neuropeptide Processing Machinery. Proteomes, 6(4):(2018) [pubmed]

curator keyword: Biological

submitter keyword: peptidylglycine -amidating monooxygenase, cilia, mating, signal peptide, prohormone convertase, carboxypeptidase, matrix metalloproteinase, subtilisin, pherophorin

Betty A. Eipper
contact affiliation	Professor, Department of Molecular Biology and Biophysics Molecular Biology and Biophysics UConn Health 263 Farmington Avenue Farmington, CT 06030-3401
contact email	eipper@uchc.edu
lab head
Navin Rauniyar
contact affiliation	Yale University
contact email	navin.rauniyar@yale.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD010945
     1. Label: PRIDE project
     2. Name: Proteases Shape the Chlamydomonas Secretome: Comparison to Classical Neuropeptide Processing Machinery