Molecular and biochemical characterization of kettin in Caenorhabditis elegans
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Kettin is a unique member of the connectin/titin family of muscle elastic proteins, which has repetitive immunoglobulin-like domains that are separated by weakly conserved linker sequences. In striated muscles of insects and crayfish, kettin binds to actin filaments and localizes to the Z-disc and its adjacent region in the I-band. Recent sequence analysis of invertebrate connectin/titin (also known as SLS proteins) has revealed that kettin is a splice variant of connectin/titin. In contrast, in the nematode Caenorhabditis elegans, the kettin gene is independent of the genes for other connectin/titin-related proteins. Immunofluorescent localization of kettin shows that it localizes to the I-bands in the obliquely striated body wall muscle. Therefore, C. elegans is an attractive model system to study specific functions of kettin in muscle cells.
KeywordsCaenorhabditis Elegans Nematode Caenorhabditis Elegans Body Wall Muscle Recent Sequence Analysis Entire cDNA Sequence
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This work is dedicated to the memory of Professor Koscak Maruyama. We are grateful to Pamela Hoppe and Robert Waterston for their gifts of the monoclonal antibodies, MH24, MH42 and MH44, Henry Epstein for his gift of the monoclonal antibody 5.6, and Laurent Segalat for his gift of the dys-1 null mutant. Wild-type C. elegans strain N2 was provided by the Caenorhabditis Genetics Center, which is funded by the National Institute of Health National Center for Research Resources. This work was supported by a grant from the National Institute of Health (R01 AR48615) to S. O.
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