| Title: | Proteases Shape the Chlamydomonas Secretome: Comparison to Classical Neuropeptide Processing Machinery |
| Author(s): | Luxmi R; Blaby-Haas C; Kumar D; Rauniyar N; King SM; Mains RE; Eipper BA; |
| Address: | "Department of Neuroscience, University of Connecticut Health Center, Farmington, CT 06030-3401, USA. luxmi@uchc.edu. Department of Biology, Brookhaven National Laboratory, Upton, NY 11973-5000, USA. mains@uchc.edu. Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT 06030-3305, USA. dhivya.kumar@ucsf.edu. W.M. Keck Biotechnology Resource Laboratory, Yale University, New Haven, CT 06511-6624, USA. cblaby@bnl.gov. Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT 06030-3305, USA. king@uchc.edu. Department of Neuroscience, University of Connecticut Health Center, Farmington, CT 06030-3401, USA. navin.rauniyar@yale.edu. Department of Neuroscience, University of Connecticut Health Center, Farmington, CT 06030-3401, USA. eipper@uchc.edu. Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT 06030-3305, USA. eipper@uchc.edu" |
| ISSN/ISBN: | 2227-7382 (Print) 2227-7382 (Electronic) 2227-7382 (Linking) |
| Abstract: | "The recent identification of catalytically active peptidylglycine alpha-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). We identified prototypical neuropeptide precursors and essential peptide processing enzymes (subtilisin-like prohormone convertases and carboxypeptidase B-like enzymes) in the C. reinhardtii genome. Reasoning that sexual reproduction by C. reinhardtii requires extensive communication between cells, we used mass spectrometry 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, and those that had been 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 secretome. Several pherophorins, ECM glycoproteins homologous to the Volvox sex-inducing pheromone, were present; most contained typical peptide processing sites, and many 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" |
| Keywords: | carboxypeptidase cilia mating matrix metalloproteinase peptidylglycine alpha-amidating monooxygenase pherophorin prohormone convertase signal peptide subtilisin; |
| Notes: | "PubMed-not-MEDLINELuxmi, Raj Blaby-Haas, Crysten Kumar, Dhivya Rauniyar, Navin King, Stephen M Mains, Richard E Eipper, Betty A eng Office of Science and Office of Biological and Environmental Research/U.S. Department of Energy/ GM051293/National Institutes of Health/ DK032949/National Institutes of Health/ P30 DA018343/DA/NIDA NIH HHS/ DA018343/National Institutes of Health/ 1S100DOD018034/National Institutes of Health/ R01 DK032949/DK/NIDDK NIH HHS/ R01 GM051293/GM/NIGMS NIH HHS/ Switzerland 2018/09/27 Proteomes. 2018 Sep 23; 6(4):36. doi: 10.3390/proteomes6040036" |
