Mechanism of egg envelope digestion by hatching enzymes, HCE and LCE in medaka, Oryzias latipes.
Mechanism of egg envelope digestion by hatching enzymes, HCE and LCE in medaka, Oryzias latipes.
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DOI:
10.1093/jb/mvq086
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发表时间:
2010-10
影响因子:
2.7
通讯作者:
S. Yasumasu;M. Kawaguchi;S. Ouchi;K. Sano;K. Murata;H. Sugiyama;T. Akema;I. Iuchi
中科院分区:
文献类型:
--
作者:
S. Yasumasu;M. Kawaguchi;S. Ouchi;K. Sano;K. Murata;H. Sugiyama;T. Akema;I. Iuchi
Hatching of medaka embryos from the fertilized egg envelope involves two enzymes, HCE and LCE. HCE swells the envelope and then LCE completely dissolves it. We determined HCE and LCE cleavage sites on the egg envelope that are primarily constructed of two groups of subunit proteins, ZI-1,2 and ZI-3. HCE and LCE cleaved different target sequences on the egg envelope proteins but shared one common cleavage site. HCE cleaved the N-terminal region of ZI-1,2 and ZI-3, mainly the Pro-Xaa-Yaa repeat sequence of ZI-1,2 into hexapeptides, but not the site within a zona pellucida (ZP) domain that is considered to be the core structure of the egg envelope. The cleavage of these N-terminal regions results in swelling and softening of the envelope. LCE cleaved the middle of the ZP domain of ZI-1,2, in addition to the upstream of the trefoil domain of ZI-1,2 and the ZP domain of ZI-3. This middle site is in the intervening sequence connecting two subdomains of the ZP domain. Cleaving this site would result in the solubilization of the swollen egg envelope by the disruption of the filamentous structure that is thought to be formed by the non-covalent polymerization of ZP domains.