Protein structural domains in the Caenorhabditis elegans unc-54 myosin heavy chain gene are not separated by introns

Proc Natl Acad Sci U S A. 1983 Jul;80(14):4253-7. doi: 10.1073/pnas.80.14.4253.


The 1,966-amino acid unc-54 myosin heavy chain sequence was determined from DNA sequence studies of the cloned gene. The gene is split by eight short introns, 48-561 base pairs long, and appears to lack a "TATA" box at its promoter. The physical map of the gene was aligned with the genetic map by locating two point mutations and three internal deletions: 0.01 map units correspond to approximately 5 kilobases. Comparison of the unc-54 protein sequence with the sequence of a second myosin heavy chain from nematode, indicates that the globular head sequence S-1 is more highly conserved than the alpha-helical coiled-coil rod. Major sites of proteolysis in S-1 are associated with variable sequences that have the characteristics of surface loops. In both genes there is no correlation between the positions of introns and the major protein structural domains.

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Animals
  • Base Sequence*
  • Caenorhabditis / genetics*
  • Chromosome Deletion
  • Genes*
  • Mutation
  • Myosins / genetics*
  • Protein Binding
  • Protein Conformation


  • Adenosine Triphosphate
  • Myosins

Associated data

  • GENBANK/J01050