Regulated secretion of a serine protease that activates an extracellular matrix-degrading metalloprotease during fertilization in Chlamydomonas

• Published in: The Journal of cell biology 1989-10, Vol.109 (4), p.1689-1694
• Main Authors: Snell, W.J. (University of Texas Southwestern Medical School, Dallas, TX), Eskue, W.A, Buchanan, M.J
• Format: Article
• Language: English
• Subjects: ALGAE; ALGUE; Analytical, structural and metabolic biochemistry; Biological and medical sciences; Bucladesine - pharmacology; Cell walls; Cells; Chlamydomonas - drug effects; Chlamydomonas - enzymology; Chlamydomonas - physiology; CHLAMYDOMONAS REINHARDTII; Cyclic AMP - physiology; Enzymes; Enzymes and enzyme inhibitors; Extracellular Matrix - physiology; FECONDATION; FECUNDACION; FERTILIZATION; Fundamental and applied biological sciences. Psychology; GAMETE; GAMETES; GAMETOS; Homeostasis; Hydrolases; Immunoblotting; Kinetics; lysin; Metalloendopeptidases - metabolism; metalloproteinase; Molecular Weight; Mucoproteins - metabolism; Mucoproteins - physiology; Periplasm; PROTEASAS; PROTEASE; PROTEASES; Room temperature; SECRECION; SECRETION; Serine Endopeptidases - metabolism; serine proteinase
• ISSN: 0021-9525; 1540-8140
• DOI: 10.1083/jcb.109.4.1689

During fertilization in the biflagellated alga, Chlamydomonas reinhardtii, gametes of opposite mating types adhere to each other via agglutinin molecules located on their flagellar surfaces, generating a sexual signal that induces several cellular responses including cell wall release. This cell contact-generated signal is mediated by cAMP and release of the wall, which is devoid of cellulose and contains several hydroxyproline-rich glycoproteins, is due to the activation of a metalloprotease, lysin. Although we originally assumed that lysin would be stored intracellularly in a compartment structurally separate from its substrate, recently we showed that lysin is stored in the periplasm as an inactive, higher relative molecular mass precursor, prolysin (Buchanan, M. J., S. H. Imam, W. A. Eskue, and W. J. Snell. 1989. J. Cell Biol. 108:199-207). Here we show that conversion of prolysin to lysin is due to a cellular, nonperiplasmic enzyme that has the properties of a serine protease. Release of this serine protease into the periplasm is induced by incubation of gametes in dibutyryl cAMP. This may be one of the few examples of regulated secretion of a protease in a eucaryotic microorganism and a novel example of regulated secretion in a plant system.