Sperm protein "DE" mediates gamete fusion through an evolutionarily conserved site of the CRISP family
The first member of the cysteine-rich secretory protein (CRISP) family was described by our laboratory in the rat epididymis, and it is known as DE or CRISP-1. Since then, numerous CRISPs exhibiting a high amino acid sequence similarity have been identified in animals, plants and fungi, although the...
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todo:paper_00121606_v297_n1_p228_Ellerman2023-10-03T14:10:17Z Sperm protein "DE" mediates gamete fusion through an evolutionarily conserved site of the CRISP family Ellerman, D.A. Cohen, D.J. Da Ros, V.G. Morgenfeld, M.M. Busso, D. Cuasnicú, P.S. CRISP Egg Fertilization Gamete fusion Sperm amino acid cysteine secretory protein synthetic peptide amino terminal sequence animal cell article binding affinity binding site controlled study deletion mutant egg female gamete genetic conservation human male mouse nonhuman priority journal protein binding protein function rat sperm structure activity relation Animalia Fungi The first member of the cysteine-rich secretory protein (CRISP) family was described by our laboratory in the rat epididymis, and it is known as DE or CRISP-1. Since then, numerous CRISPs exhibiting a high amino acid sequence similarity have been identified in animals, plants and fungi, although their functions remain largely unknown. CRISP-1 proteins are candidates to mediate gamete fusion in the rat, mouse and human through their binding to complementary sites on the egg surface. To elucidate the molecular mechanisms underlying CRISP-1 function, in the present work, deletion mutants of protein DE were generated and examined for their ability to bind to the rat egg and interfere with gamete fusion. Results revealed that the egg-binding ability of DE resides within a 45-amino acid N-terminal region containing the two motifs of the CRISP family named Signature 1 and Signature 2. Subsequent assays using synthetic peptides and other CRISPs support that the egg-binding site of DE falls in the 12-amino-acid region corresponding to Signature 2. The interesting finding that the binding site of DE resides in an evolutionarily conserved region of the molecule provides novel information on the molecular mechanisms underlying CRISP-1 function in gamete fusion with important implications on the structure-function relationship of other members of the widely distributed CRISP family. © 2006 Elsevier Inc. All rights reserved. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00121606_v297_n1_p228_Ellerman |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
CRISP Egg Fertilization Gamete fusion Sperm amino acid cysteine secretory protein synthetic peptide amino terminal sequence animal cell article binding affinity binding site controlled study deletion mutant egg female gamete genetic conservation human male mouse nonhuman priority journal protein binding protein function rat sperm structure activity relation Animalia Fungi |
| spellingShingle |
CRISP Egg Fertilization Gamete fusion Sperm amino acid cysteine secretory protein synthetic peptide amino terminal sequence animal cell article binding affinity binding site controlled study deletion mutant egg female gamete genetic conservation human male mouse nonhuman priority journal protein binding protein function rat sperm structure activity relation Animalia Fungi Ellerman, D.A. Cohen, D.J. Da Ros, V.G. Morgenfeld, M.M. Busso, D. Cuasnicú, P.S. Sperm protein "DE" mediates gamete fusion through an evolutionarily conserved site of the CRISP family |
| topic_facet |
CRISP Egg Fertilization Gamete fusion Sperm amino acid cysteine secretory protein synthetic peptide amino terminal sequence animal cell article binding affinity binding site controlled study deletion mutant egg female gamete genetic conservation human male mouse nonhuman priority journal protein binding protein function rat sperm structure activity relation Animalia Fungi |
| description |
The first member of the cysteine-rich secretory protein (CRISP) family was described by our laboratory in the rat epididymis, and it is known as DE or CRISP-1. Since then, numerous CRISPs exhibiting a high amino acid sequence similarity have been identified in animals, plants and fungi, although their functions remain largely unknown. CRISP-1 proteins are candidates to mediate gamete fusion in the rat, mouse and human through their binding to complementary sites on the egg surface. To elucidate the molecular mechanisms underlying CRISP-1 function, in the present work, deletion mutants of protein DE were generated and examined for their ability to bind to the rat egg and interfere with gamete fusion. Results revealed that the egg-binding ability of DE resides within a 45-amino acid N-terminal region containing the two motifs of the CRISP family named Signature 1 and Signature 2. Subsequent assays using synthetic peptides and other CRISPs support that the egg-binding site of DE falls in the 12-amino-acid region corresponding to Signature 2. The interesting finding that the binding site of DE resides in an evolutionarily conserved region of the molecule provides novel information on the molecular mechanisms underlying CRISP-1 function in gamete fusion with important implications on the structure-function relationship of other members of the widely distributed CRISP family. © 2006 Elsevier Inc. All rights reserved. |
| format |
JOUR |
| author |
Ellerman, D.A. Cohen, D.J. Da Ros, V.G. Morgenfeld, M.M. Busso, D. Cuasnicú, P.S. |
| author_facet |
Ellerman, D.A. Cohen, D.J. Da Ros, V.G. Morgenfeld, M.M. Busso, D. Cuasnicú, P.S. |
| author_sort |
Ellerman, D.A. |
| title |
Sperm protein "DE" mediates gamete fusion through an evolutionarily conserved site of the CRISP family |
| title_short |
Sperm protein "DE" mediates gamete fusion through an evolutionarily conserved site of the CRISP family |
| title_full |
Sperm protein "DE" mediates gamete fusion through an evolutionarily conserved site of the CRISP family |
| title_fullStr |
Sperm protein "DE" mediates gamete fusion through an evolutionarily conserved site of the CRISP family |
| title_full_unstemmed |
Sperm protein "DE" mediates gamete fusion through an evolutionarily conserved site of the CRISP family |
| title_sort |
sperm protein "de" mediates gamete fusion through an evolutionarily conserved site of the crisp family |
| url |
http://hdl.handle.net/20.500.12110/paper_00121606_v297_n1_p228_Ellerman |
| work_keys_str_mv |
AT ellermanda spermproteindemediatesgametefusionthroughanevolutionarilyconservedsiteofthecrispfamily AT cohendj spermproteindemediatesgametefusionthroughanevolutionarilyconservedsiteofthecrispfamily AT darosvg spermproteindemediatesgametefusionthroughanevolutionarilyconservedsiteofthecrispfamily AT morgenfeldmm spermproteindemediatesgametefusionthroughanevolutionarilyconservedsiteofthecrispfamily AT bussod spermproteindemediatesgametefusionthroughanevolutionarilyconservedsiteofthecrispfamily AT cuasnicups spermproteindemediatesgametefusionthroughanevolutionarilyconservedsiteofthecrispfamily |
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