HCE, a constituent of the hatching enzymes of Oryzias latipes embryos, releases unique proline-rich polypeptides from its natural substrate, the hardened chorion.
HCE, a constituent protease of the hatching enzymes of Oryzias latipes embryos [1,2], releases unique proline-rich polypeptides from its natural substrate, the hardened chorion. The polypeptides consist of repeats of Pro-X-Y, mainly Pro-Glx-X. In addition, the polypeptides contain abundant gamma-glutamyl epsilon-lysine isopeptides which are regarded to be responsible for chorion hardening. These findings suggest that HCE recognizes specific site(s) of the chorion, releases the proline-rich polypeptides from it, and makes the substrate accessible to LCE, another protease of the hatching enzymes.
Lee
K S
KS
Life Science Institute, Sophia University, Tokyo, Japan.
Yasumasu
S
S
Nomura
K
K
Iuchi
I
I
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002823:Chorion / Q000378:metabolism*; D002850:Chromatography, Gel; D008666:Metalloendopeptidases / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009990:Oryzias / Q000196:embryology*; D010455:Peptides / Q000032:analysis / Q000737:chemistry / Q000378:metabolism*; D011392:Proline / Q000032:analysis*; D012091:Repetitive Sequences, Nucleic Acid
D000596:Amino Acids; D010455:Peptides; D011392:Proline; D008666:Metalloendopeptidases; C024344:envelysin