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Novel conserved structural domains of acrosome reaction‐inducing substance are widespread in invertebrates
Author(s) -
Naruse Masahiro,
Ishikawa Riho,
Sakaya Hiroshi,
Moriyama Hideaki,
Hoshi Motonori,
Matsumoto Midori
Publication year - 2011
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/mrd.21274
Subject(s) - biology , starfish , acrosome reaction , sperm , echinoderm , acrosome , marine invertebrates , human fertilization , microbiology and biotechnology , genetics , biochemistry , ecology
In the starfish Asterias amurensis , acrosome reaction inducing substance (ARIS) is the main factor responsible for allowing sperm to recognize the egg jelly and begin the acrosome reaction (AR). ARIS is a large proteoglycan‐like molecule, and its pentasaccharide repeat, Fragment 1 (Fr. 1), is responsible for inducing AR. Here, we investigated the primary structure of ARIS for the first time in order to improve our understanding of its functionality. Electrophoretic analysis revealed that ARIS is a complex of three proteins, all of which are modified by the Fr. 1 sugar chain. Sequencing indicated that there are two novel, conserved domains in all three ARIS proteins: ARIS N‐terminus (AR‐N) and ARIS C‐terminus (AR‐C) domains. We also found that other echinoderms possess ARIS proteins that are capable of inducing the AR for homologous sperm, indicating that ARIS proteins may be a ubiquitous component for echinoderm fertilization. Moreover, we identified ARIS‐like genes from Ctenophora to Protochordata. Mol. Reprod. Dev. 78:57–66, 2011. © 2010 Wiley‐Liss, Inc.