Cloning and characterization of Xenopus dicalcin, a novel S100-like calcium-binding protein in Xenopus eggs.
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.
Miwa
Naofumi
N
Department of Physiology, School of Medicine, Toho University, Ohta-ku, Tokyo, Japan. nmiwa@med.toho-u.ac.jp
Shinmyo
Yukiko
Y
Kawamura
Satoru
S
D000595:Amino Acid Sequence / Q000235:genetics; D000818:Animals; D001345:Autoradiography; D001483:Base Sequence / Q000235:genetics; D002135:Calcium-Binding Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D003001:Cloning, Molecular; D017124:Conserved Sequence; D018076:DNA, Complementary; D020832:EF Hand Motifs / Q000235:genetics; D005260:Female; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009865:Oocytes / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism; D009418:S100 Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D014018:Tissue Distribution; D014981:Xenopus; D029867:Xenopus Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism
D002135:Calcium-Binding Proteins; D018076:DNA, Complementary; D012333:RNA, Messenger; D009418:S100 Proteins; C525113:S100A11 protein, Xenopus; D029867:Xenopus Proteins