Ovoperoxidase assembly into the sea urchin fertilization envelope and dityrosine crosslinking - PubMed (original) (raw)

Ovoperoxidase assembly into the sea urchin fertilization envelope and dityrosine crosslinking

E S Kay et al. Dev Biol. 1987 Jun.

Abstract

Ovoperoxidase, the enzyme implicated in hardening the extracellular coat of the fertilized sea urchin egg, is inserted into the assembling uncrosslinked (soft) fertilization membrane via specific interactions with a protein, proteoliaisin (P. Weidman, E. Kay, and B. M. Shapiro (1985). J. Cell. Biol. 100, 938-946), and the vitelline scaffold. Dityrosine crosslinks introduced by ovoperoxidase have been postulated to harden the assembled structure from such indirect data as the discovery of dityrosine in hard fertilization membranes (Foerder and B. M. Shapiro (1977). Proc. Natl. Acad. Sci. USA 74, 4214-4128; H. G. Hall (1978). Cell 15, 343-355). In this report, we show directly that soft fertilization membranes (SFM) contain no dityrosine residues but acquire these crosslinks in vitro only during hardening. In vitro hardening alters the susceptibility of the fertilization membrane to disruption in cation-depleted solutions and in detergent; the kinetics of these phenomena are all similar to those of hardening in vivo. Ovoperoxidase substrates were identified as a class of high-molecular-weight proteins of SFM by polyacrylamide gel electrophoresis after in vitro hardening or after an ovoperoxidase-catalyzed radioiodination reaction. The specificity of ovoperoxidase for particular substrates decreased once it was no longer associated with these polypeptides within the SFM. Moreover, after disruption of the SFM, ovoperoxidase had an increased capacity to iodinate an exogenous protein, myoglobin. These data suggest that assembly of ovoperoxidase into a specific locus within the soft fertilization membrane provides a regulatory mechanism to guarantee the crosslinking of only certain appropriately juxtaposed tyrosyl residues in the assembled structure.

PubMed Disclaimer

Cited by

Hierarchies of protein cross-linking in the extracellular matrix: involvement of an egg surface transglutaminase in early stages of fertilization envelope assembly.
Battaglia DE, Shapiro BM. Battaglia DE, et al. J Cell Biol. 1988 Dec;107(6 Pt 1):2447-54. doi: 10.1083/jcb.107.6.2447. J Cell Biol. 1988. PMID: 2904448 Free PMC article.
Direct membrane retrieval into large vesicles after exocytosis in sea urchin eggs.
Whalley T, Terasaki M, Cho MS, Vogel SS. Whalley T, et al. J Cell Biol. 1995 Dec;131(5):1183-92. doi: 10.1083/jcb.131.5.1183. J Cell Biol. 1995. PMID: 8522582 Free PMC article.
Major chorion proteins and their crosslinking during chorion hardening in Aedes aegypti mosquitoes.
Li JS, Li J. Li JS, et al. Insect Biochem Mol Biol. 2006 Dec;36(12):954-64. doi: 10.1016/j.ibmb.2006.09.006. Epub 2006 Sep 23. Insect Biochem Mol Biol. 2006. PMID: 17098170 Free PMC article.
Extracellular matrix modifications at fertilization: regulation of dityrosine crosslinking by transamidation.
Wong JL, Wessel GM. Wong JL, et al. Development. 2009 Jun;136(11):1835-47. doi: 10.1242/dev.030775. Epub 2009 Apr 29. Development. 2009. PMID: 19403662 Free PMC article.
Ascospore formation in the yeast Saccharomyces cerevisiae.
Neiman AM. Neiman AM. Microbiol Mol Biol Rev. 2005 Dec;69(4):565-84. doi: 10.1128/MMBR.69.4.565-584.2005. Microbiol Mol Biol Rev. 2005. PMID: 16339736 Free PMC article. Review.

Ovoperoxidase assembly into the sea urchin fertilization envelope and dityrosine crosslinking - PubMed (original) (raw)