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Cho, JH, Oh, YS, Park, KW, Yu, J, Choi, KY, Shin, JY, Kim, DH, Park, WJ, Hamada, T, Kagawa, H, Maryon, EB, Bandyopadhyay, J and Ahnn, J (2000) Calsequestrin, a calcium sequestering protein localized at the sarcoplasmic reticulum, is not essential for body-wall muscle function in Caenorhabditis elegans. J. Cell. Sci. 113 ( Pt 22):3947-58
Calsequestrin is the major calcium-binding protein of cardiac and skeletal muscles whose function is to sequester Ca(2+ )in the lumen of the sarcoplasmic reticulum (SR). Here we describe the identification and functional characterization of a C. elegans calsequestrin gene (csq-1). CSQ-1 shows moderate similarity (50% similarity, 30% identity) to rabbit skeletal calsequestrin. Unlike mammals, which have two different genes encoding cardiac and fast-twitch skeletal muscle isoforms, csq-1 is the only calsequestrin gene in the C. elegans genome. We show that csq-1 is highly expressed in the body-wall muscles, beginning in mid-embryogenesis and maintained through the adult stage. In body-wall muscle cells, CSQ-1 is localized to sarcoplasmic membranes surrounding sarcomeric structures, in the regions where ryanodine receptors (UNC-68) are located. Mutation in UNC-68 affects CSQ-1 localization, suggesting that the two possibly interact in vivo. Genetic analyses of chromosomal deficiency mutants deleting csq-1 show that CSQ-1 is not essential for initiation of embryonic muscle formation and contraction. Furthermore, double-stranded RNA injection resulted in animals completely lacking CSQ-1 in body-wall muscles with no observable defects in locomotion. These findings suggest that although CSQ-1 is one of the major calcium-binding proteins in the body-wall muscles of C. elegans, it is not essential for body-wall muscle formation and contraction.
Amino Acid Sequence; Animals; Base Sequence; Caenorhabditis elegans/genetics; Caenorhabditis elegans/physiology; Calcium/metabolism; Calsequestrin/chemistry; Calsequestrin/genetics; Calsequestrin/metabolism; Chromosome Mapping; Cloning, Molecular; Gene Deletion; Genes, Helminth; Humans; Mammals; Molecular Sequence Data; Muscle, Skeletal/physiology; Rabbits; Recombinant Proteins/biosynthesis; Recombinant Proteins/chemistry; Sarcoplasmic Reticulum/physiology; Sarcoplasmic Reticulum/ultrastructure; Sequence Alignment; Sequence Homology, Amino Acid