cDNA cloning and predicted primary structure of scallop sarcoplasmic reticulum Ca2+-ATPase

Yoshiaki Nagata; Taibo Yamamoto; Masatsugu Ema; Junsei Mimura; Yoshiaki Fujii-Kuriyama; Tomohiko Suzuki; Takahiro Furukohri; Kazuhiko Konishi; Dai Sato; Genichi Tajima; Jun Nakamura

doi:10.1016/S0305-0491(98)00055-8

cDNA cloning and predicted primary structure of scallop sarcoplasmic reticulum Ca²⁺-ATPase

Yoshiaki Nagata, Taibo Yamamoto, Masatsugu Ema, Junsei Mimura, Yoshiaki Fujii-Kuriyama, Tomohiko Suzuki, Takahiro Furukohri, Kazuhiko Konishi, Dai Sato, Genichi Tajima, Jun Nakamura

IEHE - Division of Developmental Research in Education Programs

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6 Citations (Scopus)

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. Copyright (C) 1998 Elsevier Science Inc.

Original language	English
Pages (from-to)	777-785
Number of pages	9
Journal	Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume	119
Issue number	4
DOIs	https://doi.org/10.1016/S0305-0491(98)00055-8
Publication status	Published - 1998

Keywords

Adductor muscle
Amino acid sequence
Ca-ATPase
Cross-striated muscle
Invertebrate
Molecular evolution
Mollusca
Nucleotide sequence
cDNA-cloning

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Nagata, Y., Yamamoto, T., Ema, M., Mimura, J., Fujii-Kuriyama, Y., Suzuki, T., Furukohri, T., Konishi, K., Sato, D., Tajima, G., & Nakamura, J. (1998). cDNA cloning and predicted primary structure of scallop sarcoplasmic reticulum Ca²⁺-ATPase. Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, 119(4), 777-785. https://doi.org/10.1016/S0305-0491(98)00055-8

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title = "cDNA cloning and predicted primary structure of scallop sarcoplasmic reticulum Ca2+-ATPase",

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. Copyright (C) 1998 Elsevier Science Inc.",

keywords = "Adductor muscle, Amino acid sequence, Ca-ATPase, Cross-striated muscle, Invertebrate, Molecular evolution, Mollusca, Nucleotide sequence, cDNA-cloning",

author = "Yoshiaki Nagata and Taibo Yamamoto and Masatsugu Ema and Junsei Mimura and Yoshiaki Fujii-Kuriyama and Tomohiko Suzuki and Takahiro Furukohri and Kazuhiko Konishi and Dai Sato and Genichi Tajima and Jun Nakamura",

year = "1998",

doi = "10.1016/S0305-0491(98)00055-8",

language = "English",

volume = "119",

pages = "777--785",

journal = "Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology",

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Nagata, Y, Yamamoto, T, Ema, M, Mimura, J, Fujii-Kuriyama, Y, Suzuki, T, Furukohri, T, Konishi, K, Sato, D, Tajima, G & Nakamura, J 1998, 'cDNA cloning and predicted primary structure of scallop sarcoplasmic reticulum Ca²⁺-ATPase', Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, vol. 119, no. 4, pp. 777-785. https://doi.org/10.1016/S0305-0491(98)00055-8

TY - JOUR

T1 - cDNA cloning and predicted primary structure of scallop sarcoplasmic reticulum Ca2+-ATPase

AU - Nagata, Yoshiaki

AU - Yamamoto, Taibo

AU - Ema, Masatsugu

AU - Mimura, Junsei

AU - Fujii-Kuriyama, Yoshiaki

AU - Suzuki, Tomohiko

AU - Furukohri, Takahiro

AU - Konishi, Kazuhiko

AU - Sato, Dai

AU - Tajima, Genichi

AU - Nakamura, Jun

PY - 1998

Y1 - 1998

N2 - 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. Copyright (C) 1998 Elsevier Science Inc.

AB - 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. Copyright (C) 1998 Elsevier Science Inc.

KW - Adductor muscle

KW - Amino acid sequence

KW - Ca-ATPase

KW - Cross-striated muscle

KW - Invertebrate

KW - Molecular evolution

KW - Mollusca

KW - Nucleotide sequence

KW - cDNA-cloning

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AN - SCOPUS:13144283614

SN - 1096-4959

VL - 119

SP - 777

EP - 785

JO - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

JF - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

IS - 4

ER -

cDNA cloning and predicted primary structure of scallop sarcoplasmic reticulum Ca²⁺-ATPase

Abstract

Keywords

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