BINDIN GENE FROM THE KUMAMOTO OYSTER CRASSOSTREA SIKAMEA, AND DIVERGENCE OF THE FUCOSE LECTIN REPEATS OF BINDIN AMONG THREE SPECIES OF CRASSOSTREA
Bindin is a major protein packaged as insoluble granules in sperm acrosomes. It may be responsible for species-specific recognition and binding of sperm to a glycoprotein receptor on the surface of eggs. The putative functional region of bindin is a fucose-binding lectin (F-lectin) domain. We cloned...
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ftchinacasciocas:oai:ir.qdio.ac.cn:337002/11997 2023-05-15T15:58:32+02:00 BINDIN GENE FROM THE KUMAMOTO OYSTER CRASSOSTREA SIKAMEA, AND DIVERGENCE OF THE FUCOSE LECTIN REPEATS OF BINDIN AMONG THREE SPECIES OF CRASSOSTREA Wu, Qi Xu, Fei Ba, Yongbo Li, Li Zhang, Guofan 2011-04-01 http://ir.qdio.ac.cn/handle/337002/11998 https://doi.org/10.2983/035.030.0109 英语 eng JOURNAL OF SHELLFISH RESEARCH Wu, Qi; Xu, Fei; Ba, Yongbo; Li, Li; Zhang, Guofan.BINDIN GENE FROM THE KUMAMOTO OYSTER CRASSOSTREA SIKAMEA, AND DIVERGENCE OF THE FUCOSE LECTIN REPEATS OF BINDIN AMONG THREE SPECIES OF CRASSOSTREA,JOURNAL OF SHELLFISH RESEARCH,2011,30(1):55-64 http://ir.qdio.ac.cn/handle/337002/11998 doi:10.2983/035.030.0109 Crassostrea Crassostrea Gigas Crassostrea Sikamea Crassostrea Angulata Fucose Lectin Repeats Sperm-egg Interaction Positive Selection Fisheries Marine & Freshwater Biology Article 期刊论文 2011 ftchinacasciocas https://doi.org/10.2983/035.030.0109 2022-06-27T05:34:17Z Bindin is a major protein packaged as insoluble granules in sperm acrosomes. It may be responsible for species-specific recognition and binding of sperm to a glycoprotein receptor on the surface of eggs. The putative functional region of bindin is a fucose-binding lectin (F-lectin) domain. We cloned a novel bindin gene from the Kumamoto oyster Crassostrea sikamea by 3` and 5` RACE. The full-length cDNA of C. sikamea bindin was 1,134 bp, with a 774-bp open reading frame encoding 257 amino acids. The deduced amino acid sequence contained a putative signal peptide of 24 amino acids. The length of the bindin genomic DNA we obtained was 5,353 bp, containing 4 exons and 3 introns. We studied F-lectin repeats of the bindin gene from 3 species of Crassostrea to detect the relationship between them and found 11, 2, and 5 haplotypes from C. sikamea, Crassostrea angulata, and Crassostrea gigas, respectively. Phylogenetic trees showed a closer relationship between C. gigas and C. angulata than between C. gigas and C. sikamea. Two haplotypes of C. angulata fell into 2 different clades, one in the C. gigas clade and the other in the C. sikamea clade. Deduced amino acid sequences and hydropathy plots were considerably similar among these species, indicating the close resemblance in the tertiary structure of bindin proteins. To test for selection, we compared the number of nonsynonymous substitutions and synonymous substitutions per nucleotide site among the 18 F-lectin haplotypes. This analysis identified 7 positively selected positions (P > 95%) among 18 haplotypes from the 3 species, all located on the F-lectin binding face around the 3 residues that are specifically involved in binding fucose (H37. R64, and R70). We hypothesize that these 7 clustered amino acids may be related to species recognition and thus could impose selective pressure on bindin divergence. Bindin is a major protein packaged as insoluble granules in sperm acrosomes. It may be responsible for species-specific recognition and binding of sperm to a ... Article in Journal/Newspaper Crassostrea gigas Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR Journal of Shellfish Research 30 1 55 64 |
institution |
Open Polar |
collection |
Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR |
op_collection_id |
ftchinacasciocas |
language |
English |
topic |
Crassostrea Crassostrea Gigas Crassostrea Sikamea Crassostrea Angulata Fucose Lectin Repeats Sperm-egg Interaction Positive Selection Fisheries Marine & Freshwater Biology |
spellingShingle |
Crassostrea Crassostrea Gigas Crassostrea Sikamea Crassostrea Angulata Fucose Lectin Repeats Sperm-egg Interaction Positive Selection Fisheries Marine & Freshwater Biology Wu, Qi Xu, Fei Ba, Yongbo Li, Li Zhang, Guofan BINDIN GENE FROM THE KUMAMOTO OYSTER CRASSOSTREA SIKAMEA, AND DIVERGENCE OF THE FUCOSE LECTIN REPEATS OF BINDIN AMONG THREE SPECIES OF CRASSOSTREA |
topic_facet |
Crassostrea Crassostrea Gigas Crassostrea Sikamea Crassostrea Angulata Fucose Lectin Repeats Sperm-egg Interaction Positive Selection Fisheries Marine & Freshwater Biology |
description |
Bindin is a major protein packaged as insoluble granules in sperm acrosomes. It may be responsible for species-specific recognition and binding of sperm to a glycoprotein receptor on the surface of eggs. The putative functional region of bindin is a fucose-binding lectin (F-lectin) domain. We cloned a novel bindin gene from the Kumamoto oyster Crassostrea sikamea by 3` and 5` RACE. The full-length cDNA of C. sikamea bindin was 1,134 bp, with a 774-bp open reading frame encoding 257 amino acids. The deduced amino acid sequence contained a putative signal peptide of 24 amino acids. The length of the bindin genomic DNA we obtained was 5,353 bp, containing 4 exons and 3 introns. We studied F-lectin repeats of the bindin gene from 3 species of Crassostrea to detect the relationship between them and found 11, 2, and 5 haplotypes from C. sikamea, Crassostrea angulata, and Crassostrea gigas, respectively. Phylogenetic trees showed a closer relationship between C. gigas and C. angulata than between C. gigas and C. sikamea. Two haplotypes of C. angulata fell into 2 different clades, one in the C. gigas clade and the other in the C. sikamea clade. Deduced amino acid sequences and hydropathy plots were considerably similar among these species, indicating the close resemblance in the tertiary structure of bindin proteins. To test for selection, we compared the number of nonsynonymous substitutions and synonymous substitutions per nucleotide site among the 18 F-lectin haplotypes. This analysis identified 7 positively selected positions (P > 95%) among 18 haplotypes from the 3 species, all located on the F-lectin binding face around the 3 residues that are specifically involved in binding fucose (H37. R64, and R70). We hypothesize that these 7 clustered amino acids may be related to species recognition and thus could impose selective pressure on bindin divergence. Bindin is a major protein packaged as insoluble granules in sperm acrosomes. It may be responsible for species-specific recognition and binding of sperm to a ... |
format |
Article in Journal/Newspaper |
author |
Wu, Qi Xu, Fei Ba, Yongbo Li, Li Zhang, Guofan |
author_facet |
Wu, Qi Xu, Fei Ba, Yongbo Li, Li Zhang, Guofan |
author_sort |
Wu, Qi |
title |
BINDIN GENE FROM THE KUMAMOTO OYSTER CRASSOSTREA SIKAMEA, AND DIVERGENCE OF THE FUCOSE LECTIN REPEATS OF BINDIN AMONG THREE SPECIES OF CRASSOSTREA |
title_short |
BINDIN GENE FROM THE KUMAMOTO OYSTER CRASSOSTREA SIKAMEA, AND DIVERGENCE OF THE FUCOSE LECTIN REPEATS OF BINDIN AMONG THREE SPECIES OF CRASSOSTREA |
title_full |
BINDIN GENE FROM THE KUMAMOTO OYSTER CRASSOSTREA SIKAMEA, AND DIVERGENCE OF THE FUCOSE LECTIN REPEATS OF BINDIN AMONG THREE SPECIES OF CRASSOSTREA |
title_fullStr |
BINDIN GENE FROM THE KUMAMOTO OYSTER CRASSOSTREA SIKAMEA, AND DIVERGENCE OF THE FUCOSE LECTIN REPEATS OF BINDIN AMONG THREE SPECIES OF CRASSOSTREA |
title_full_unstemmed |
BINDIN GENE FROM THE KUMAMOTO OYSTER CRASSOSTREA SIKAMEA, AND DIVERGENCE OF THE FUCOSE LECTIN REPEATS OF BINDIN AMONG THREE SPECIES OF CRASSOSTREA |
title_sort |
bindin gene from the kumamoto oyster crassostrea sikamea, and divergence of the fucose lectin repeats of bindin among three species of crassostrea |
publishDate |
2011 |
url |
http://ir.qdio.ac.cn/handle/337002/11998 https://doi.org/10.2983/035.030.0109 |
genre |
Crassostrea gigas |
genre_facet |
Crassostrea gigas |
op_relation |
JOURNAL OF SHELLFISH RESEARCH Wu, Qi; Xu, Fei; Ba, Yongbo; Li, Li; Zhang, Guofan.BINDIN GENE FROM THE KUMAMOTO OYSTER CRASSOSTREA SIKAMEA, AND DIVERGENCE OF THE FUCOSE LECTIN REPEATS OF BINDIN AMONG THREE SPECIES OF CRASSOSTREA,JOURNAL OF SHELLFISH RESEARCH,2011,30(1):55-64 http://ir.qdio.ac.cn/handle/337002/11998 doi:10.2983/035.030.0109 |
op_doi |
https://doi.org/10.2983/035.030.0109 |
container_title |
Journal of Shellfish Research |
container_volume |
30 |
container_issue |
1 |
container_start_page |
55 |
op_container_end_page |
64 |
_version_ |
1766394280499216384 |