Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1983 Jul;80(14):4253–4257. doi: 10.1073/pnas.80.14.4253

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

J Karn, S Brenner, L Barnett
PMCID: PMC384015  PMID: 6576334

Abstract

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.

Full text

PDF

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anderson S. Shotgun DNA sequencing using cloned DNase I-generated fragments. Nucleic Acids Res. 1981 Jul 10;9(13):3015–3027. doi: 10.1093/nar/9.13.3015. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Benoist C., Chambon P. In vivo sequence requirements of the SV40 early promotor region. Nature. 1981 Mar 26;290(5804):304–310. doi: 10.1038/290304a0. [DOI] [PubMed] [Google Scholar]
  3. Berk A. J., Sharp P. A. Structure of the adenovirus 2 early mRNAs. Cell. 1978 Jul;14(3):695–711. doi: 10.1016/0092-8674(78)90252-0. [DOI] [PubMed] [Google Scholar]
  4. Brenner S. The genetics of Caenorhabditis elegans. Genetics. 1974 May;77(1):71–94. doi: 10.1093/genetics/77.1.71. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Cardinaud R. Proteolytic fragmentation of myosin: location of SH-1 and SH-2 thiols. Biochimie. 1979;61(7):807–821. doi: 10.1016/s0300-9084(79)80275-8. [DOI] [PubMed] [Google Scholar]
  6. Cochet M., Gannon F., Hen R., Maroteaux L., Perrin F., Chambon P. Organization and sequence studies of the 17-piece chicken conalbumin gene. Nature. 1979 Dec 6;282(5739):567–574. doi: 10.1038/282567a0. [DOI] [PubMed] [Google Scholar]
  7. Dugaiczyk A., Woo S. L., Lai E. C., Mace M. L., Jr, McReynolds L., O'Malley B. W. The natural ovalbumin gene contains seven intervening sequences. Nature. 1978 Jul 27;274(5669):328–333. doi: 10.1038/274328a0. [DOI] [PubMed] [Google Scholar]
  8. Elzinga M., Collins J. H. Amino acid sequence of a myosin fragment that contains SH-1, SH-2, and Ntau-methylhistidine. Proc Natl Acad Sci U S A. 1977 Oct;74(10):4281–4284. doi: 10.1073/pnas.74.10.4281. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Epstein H. F., Waterston R. H., Brenner S. A mutant affecting the heavy chain of myosin in Caenorhabditis elegans. J Mol Biol. 1974 Dec 5;90(2):291–300. doi: 10.1016/0022-2836(74)90374-x. [DOI] [PubMed] [Google Scholar]
  10. Gilbert W. Why genes in pieces? Nature. 1978 Feb 9;271(5645):501–501. doi: 10.1038/271501a0. [DOI] [PubMed] [Google Scholar]
  11. Karn J., Brenner S., Barnett L., Cesareni G. Novel bacteriophage lambda cloning vector. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5172–5176. doi: 10.1073/pnas.77.9.5172. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kramer J. M., Cox G. N., Hirsh D. Comparisons of the complete sequences of two collagen genes from Caenorhabditis elegans. Cell. 1982 Sep;30(2):599–606. doi: 10.1016/0092-8674(82)90256-2. [DOI] [PubMed] [Google Scholar]
  13. Lewin R. On the origin of introns. Science. 1982 Sep 3;217(4563):921–922. doi: 10.1126/science.7112105. [DOI] [PubMed] [Google Scholar]
  14. Lowey S., Slayter H. S., Weeds A. G., Baker H. Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation. J Mol Biol. 1969 May 28;42(1):1–29. doi: 10.1016/0022-2836(69)90483-5. [DOI] [PubMed] [Google Scholar]
  15. Lu R. C. Identification of a region susceptible to proteolysis in myosin subfragment-2. Proc Natl Acad Sci U S A. 1980 Apr;77(4):2010–2013. doi: 10.1073/pnas.77.4.2010. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. MacLeod A. R., Karn J., Brenner S. Molecular analysis of the unc-54 myosin heavy-chain gene of Caenorhabditis elegans. Nature. 1981 Jun 4;291(5814):386–390. doi: 10.1038/291386a0. [DOI] [PubMed] [Google Scholar]
  17. MacLeod A. R., Waterston R. H., Fishpool R. M., Brenner S. Identification of the structural gene for a myosin heavy-chain in Caenorhabditis elegans. J Mol Biol. 1977 Jul;114(1):133–140. doi: 10.1016/0022-2836(77)90287-x. [DOI] [PubMed] [Google Scholar]
  18. McLachlan A. D., Karn J. Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle. Nature. 1982 Sep 16;299(5880):226–231. doi: 10.1038/299226a0. [DOI] [PubMed] [Google Scholar]
  19. McLachlan A. D., Karn J. Periodic features in the amino acid sequence of nematode myosin rod. J Mol Biol. 1983 Mar 15;164(4):605–626. doi: 10.1016/0022-2836(83)90053-0. [DOI] [PubMed] [Google Scholar]
  20. Moerman D. G., Plurad S., Waterston R. H., Baillie D. L. Mutations in the unc-54 myosin heavy chain gene of Caenorhabditis elegans that alter contractility but not muscle structure. Cell. 1982 Jul;29(3):773–781. doi: 10.1016/0092-8674(82)90439-1. [DOI] [PubMed] [Google Scholar]
  21. Mount S. M. A catalogue of splice junction sequences. Nucleic Acids Res. 1982 Jan 22;10(2):459–472. doi: 10.1093/nar/10.2.459. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Pai E. F., Sachsenheimer W., Schirmer R. H., Schulz G. E. Substrate positions and induced-fit in crystalline adenylate kinase. J Mol Biol. 1977 Jul;114(1):37–45. doi: 10.1016/0022-2836(77)90281-9. [DOI] [PubMed] [Google Scholar]
  23. Sanger F., Coulson A. R., Barrell B. G., Smith A. J., Roe B. A. Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. J Mol Biol. 1980 Oct 25;143(2):161–178. doi: 10.1016/0022-2836(80)90196-5. [DOI] [PubMed] [Google Scholar]
  24. Staden R., McLachlan A. D. Codon preference and its use in identifying protein coding regions in long DNA sequences. Nucleic Acids Res. 1982 Jan 11;10(1):141–156. doi: 10.1093/nar/10.1.141. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Walker J. E., Saraste M., Runswick M. J., Gay N. J. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1982;1(8):945–951. doi: 10.1002/j.1460-2075.1982.tb01276.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Waterston R. H., Smith K. C., Moerman D. G. Genetic fine structure analysis of the myosin heavy chain gene unc-54 of Caenorhabditis elegans. J Mol Biol. 1982 Jun 15;158(1):1–15. doi: 10.1016/0022-2836(82)90447-8. [DOI] [PubMed] [Google Scholar]
  27. Weeds A. G., Pope B. Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility. J Mol Biol. 1977 Apr;111(2):129–157. doi: 10.1016/s0022-2836(77)80119-8. [DOI] [PubMed] [Google Scholar]
  28. Wozney J., Hanahan D., Morimoto R., Boedtker H., Doty P. Fine structural analysis of the chicken pro alpha 2 collagen gene. Proc Natl Acad Sci U S A. 1981 Feb;78(2):712–716. doi: 10.1073/pnas.78.2.712. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES