Abstract
To contribute to the study of the calcium-signaling mechanism of egg, we cloned and characterized a 26 kDa Ca(2+)-binding protein from Xenopus laevis eggs, a homologue of Rana catesbeiana dicalcin (renamed from p26olf) that was isolated from the olfactory epithelium. The primary structure of Xenopus dicalcin shows approximately 61% identity to that of Rana dicalcin and consists of two S100-like regions aligned in tandem, as seen in Rana dicalcin. Genomic Southern blot analysis indicated that Xenopus dicalcin is a unique orthologue of Rana dicalcin. Northern blot analysis showed that Xenopus dicalcin mRNA is expressed in Xenopus eggs and also in other tissues. These results indicated that Xenopus dicalcin is a novel S100-like Ca(2+)-binding protein in Xenopus eggs.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence / genetics
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Animals
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Autoradiography
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Base Sequence / genetics
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Calcium-Binding Proteins / chemistry
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Calcium-Binding Proteins / genetics*
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Calcium-Binding Proteins / metabolism
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Cloning, Molecular*
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Conserved Sequence
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DNA, Complementary
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EF Hand Motifs / genetics
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Female
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Molecular Sequence Data
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Molecular Weight
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Oocytes / metabolism
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RNA, Messenger / metabolism
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S100 Proteins / chemistry
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S100 Proteins / genetics*
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S100 Proteins / metabolism
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Sequence Homology, Amino Acid
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Tissue Distribution
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Xenopus
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Xenopus Proteins / chemistry
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Xenopus Proteins / genetics*
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Xenopus Proteins / metabolism
Substances
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Calcium-Binding Proteins
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DNA, Complementary
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RNA, Messenger
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S100 Proteins
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S100A11 protein, Xenopus
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Xenopus Proteins