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The pathway of myofibrillogenesis determines the interrelationship between myosin and paramyosin synthesis inCaenorhabditis elegans
Author(s) -
Glenn E. White,
Christine M. Petry,
Fred Schachat
Publication year - 2003
Publication title -
journal of experimental biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.367
H-Index - 185
eISSN - 1477-9145
pISSN - 0022-0949
DOI - 10.1242/jeb.00377
Subject(s) - caenorhabditis elegans , myosin , biology , microbiology and biotechnology , genetics , gene
Examination of null mutants in myosin B and paramyosin yields insights into the complex mechanisms that regulate expression of the three major components of Caenorhabditis elegans body-wall muscle thick filaments myosin A, myosin B and paramyosin. In the absence of myosin B, paramyosin accumulation is reduced, although neither its synthesis nor that of myosin A is affected. This implies that the interaction of myosin B with paramyosin inhibits paramyosin degradation. By contrast, the absence of paramyosin results in reduced synthesis and accumulation of myosin B but has no effect on myosin A synthesis. The non-reciprocal effects of the null mutants on turnover and synthesis are best understood as an epigenetic phenomenon that reflects the pathway of thick filament assembly. The synthesis of myosin A and paramyosin, which are involved in the initial steps of thick filament formation, is independent of myosin B; however, a properly assembled paramyosin-containing thick filament core is essential for efficient synthesis of myosin B.

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