Functions of the myosin ATP and actin binding sites are required for C. elegans thick filament assembly
Identifieur interne : 004A36 ( Main/Exploration ); précédent : 004A35; suivant : 004A37Functions of the myosin ATP and actin binding sites are required for C. elegans thick filament assembly
Auteurs : Amy Bejsovec [États-Unis] ; Philip Anderson [États-Unis]Source :
- Cell [ 0092-8674 ] ; 1990.
English descriptors
- Teeft :
- Actin, Actin binding, Actin binding site, Allele, Amino, Amino acids, Assembly defects, Atpase, Atpase activity, Bejsovec, Binding site, Biol, Caenorhabditis, Caenorhabditis elegans, Cell biol, Chain gene, Dibb, Dimer, Dominant alleles, Dominant mutations, Elegans, Filament, Filament assembly, Genomic, Globular, Independent mutations, Karn, Mhcs, Mismatch, Missense, Missense mutations, Mutant, Mutant protein, Mutation, Mutational cluster, Myosin, Myosin atpase, Myosin dimers, Nematode, Nucleotide, Nucleotide binding, Nucleotide binding consensus sequence, Nucleotide binding proteins, Personal communication, Sarcomere, Sarcomere assembly, Striated muscle, Substitution, Thick filament, Thick filament assembly, Thick filaments, Waterston.
Abstract
Abstract: 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.
Url:
DOI: 10.1016/0092-8674(90)90723-R
Affiliations:
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Le document en format XML
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<term>Actin binding</term>
<term>Actin binding site</term>
<term>Allele</term>
<term>Amino</term>
<term>Amino acids</term>
<term>Assembly defects</term>
<term>Atpase</term>
<term>Atpase activity</term>
<term>Bejsovec</term>
<term>Binding site</term>
<term>Biol</term>
<term>Caenorhabditis</term>
<term>Caenorhabditis elegans</term>
<term>Cell biol</term>
<term>Chain gene</term>
<term>Dibb</term>
<term>Dimer</term>
<term>Dominant alleles</term>
<term>Dominant mutations</term>
<term>Elegans</term>
<term>Filament</term>
<term>Filament assembly</term>
<term>Genomic</term>
<term>Globular</term>
<term>Independent mutations</term>
<term>Karn</term>
<term>Mhcs</term>
<term>Mismatch</term>
<term>Missense</term>
<term>Missense mutations</term>
<term>Mutant</term>
<term>Mutant protein</term>
<term>Mutation</term>
<term>Mutational cluster</term>
<term>Myosin</term>
<term>Myosin atpase</term>
<term>Myosin dimers</term>
<term>Nematode</term>
<term>Nucleotide</term>
<term>Nucleotide binding</term>
<term>Nucleotide binding consensus sequence</term>
<term>Nucleotide binding proteins</term>
<term>Personal communication</term>
<term>Sarcomere</term>
<term>Sarcomere assembly</term>
<term>Striated muscle</term>
<term>Substitution</term>
<term>Thick filament</term>
<term>Thick filament assembly</term>
<term>Thick filaments</term>
<term>Waterston</term>
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<front><div type="abstract" xml:lang="en">Abstract: 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.</div>
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