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cDNA cloning and predicted primary structure of scallop sarcoplasmic reticulum Ca-ATPase |
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| Authors: | Yoshiaki Nagata Taibo Yamamoto Masatsugu Ema Junsei Mimura Yoshiaki Fujii-Kuriyama Tomohiko Suzuki Takahiro Furukohri Kazuhiko Konishi Dai Sato Genichi Tajima Jun Nakamura |
| Affiliation: | aBiological Institute, Graduate School of Science, Osaka University, Toyonaka, Osaka 560, Japan;bDepartment of Chemistry, Graduate School of Science, Tohoku University, Sendai, Miyagi 980-77, Japan;cBiological Institute, Faculty of Science, Kohchi University, Akebono-machi, Kohchi 780, Japan;dFaculty of Liberal Arts, Tohokugakuin University, Izumi-ku, Sendai, Miyagi 981-3193, Japan;eBiological Institute, Graduate School of Science, Tohoku University, Sendai, Miyagi 980-77, Japan |
| Abstract: | Sarcoplasmic reticulum (SR) Ca2+-ATPase of the scallop cross-striated adductor muscle was purified with deoxycholate and digested with lysyl endopeptidase for sequencing of the digested fragments. Overlapping cDNA clones of the ATPase were isolated by screening the cDNA library with an RT-PCR product as a hybridization probe, which encodes the partial amino acid sequence of the ATPase. The predicted amino acid sequence of the ATPase contained all the partial sequences determined with the proteolytic fragments and consisted of the 993 residues with 70% overall sequence similarity to those of the SR ATPases from rabbit fast-twitch and slow-twitch muscles. An outline of the structure of the scallop ATPase molecule is predicted to mainly consist of ten transmembrane and five ‘stalk’ domains with two large cytoplasmic regions as observed with the rabbit ATPase molecules. The sequence relationship between scallop and other sarco/endoplasmic reticulum-type Ca2+-ATPases is discussed. |
| Keywords: | Invertebrate Mollusca Cross-striated muscle Adductor muscle Ca2+-ATPase cDNA-cloning Nucleotide sequence Amino acid sequence Molecular evolution |
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