Protein structural domains in the Caenorhabditis elegans unc-54 myosin heavy chain gene are not separated by introns.
AUTOR(ES)
Karn, J
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=384015Documentos Relacionados
- The Gene Structures of Spontaneous Mutations Affecting a CAENORHABDITIS ELEGANS Myosin Heavy Chain Gene
- A selection for myosin heavy chain mutants in the nematode Caenorhabditis elegans.
- An internal deletion mutant of a myosin heavy chain in Caenorhabditis elegans.
- Conserved protein domains in a myosin heavy chain gene from Dictyostelium discoideum.
- Functional Domains of the Drosophila melanogaster Muscle Myosin Heavy-Chain Gene Are Encoded by Alternatively Spliced Exons