Functions of the myosin ATP and actin binding sites are required for C. elegans thick filament assembly.
We have determined the positions and sequences of 31 dominant mutations affecting a C. elegans muscle myosin heavy chain gene. These mutations alter thick filament structure in heterozygotes by interfering with the ability of wild-type myosin to assemble into stable thick filaments. These assembly-disruptive mutations are missense alleles affecting the globular head of myosin. The most strongly dominant alleles alter highly conserved residues of the myosin ATP binding site, indicating that functions of the myosin ATPase are important for thick filament assembly. Other alleles alter the site at which myosin binds actin.
Bejsovec
A
A
Department of Genetics, University of Wisconsin, Madison 53706.
Anderson
P
P
D008841:Actin Cytoskeleton / Q000378:metabolism / Q000648:ultrastructure*; D000199:Actins / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000483:Alleles; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D002107:Caenorhabditis / Q000235:genetics* / Q000378:metabolism; D003062:Codon / Q000235:genetics; D003599:Cytoskeleton / Q000648:ultrastructure*; D005784:Gene Amplification; D005796:Genes; D008969:Molecular Sequence Data; D009132:Muscles / Q000378:metabolism* / Q000648:ultrastructure; D009154:Mutation; D015879:Myosin Subfragments / Q000235:genetics* / Q000378:metabolism; D009218:Myosins / Q000235:genetics* / Q000378:metabolism
D000199:Actins; D003062:Codon; D015879:Myosin Subfragments; D000255:Adenosine Triphosphate; D009218:Myosins