Skip to main content
PMC home page
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
. 1980 Apr;77(4):2010–2013. doi: 10.1073/pnas.77.4.2010

Identification of a region susceptible to proteolysis in myosin subfragment-2.

R C Lu
PMCID: PMC348640  PMID: 6929534

Abstract

Comparison of the NH2-terminal sequence of myosin short subfragment-2 (Mr of subunit = 37,000) and long subfragment-2 (Mr of subunit = 59,000) demonstrates that the former represents the NH2-terminal portion of the latter and suggests that the hinge region in myosin rod is in the COOH-terminal portion of the long subfragment-2.

Full text

PDF
2012

Images in this article

2011Image
on p.2011
2011Image
on p.2011
2011Image
on p.2011

Selected References

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

  1. Bálint M., Sréter F. A., Gergely J. Fragmentation of myosin by papain--studies on myosin from adult fast and slow skeletal and cardiac, and embryonic muscle. Arch Biochem Biophys. 1975 Jun;168(2):557–566. doi: 10.1016/0003-9861(75)90287-8. [DOI] [PubMed] [Google Scholar]
  2. Bálint M., Sréter F. A., Wolf I., Nagy B., Gergely J. The substructure of heavy meromyosin. The effect of Ca2+ and Mg2+ on the tryptic fragmentation of heavy meromyosin. J Biol Chem. 1975 Aug 10;250(15):6168–6177. [PubMed] [Google Scholar]
  3. CRESTFIELD A. M., MOORE S., STEIN W. H. The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J Biol Chem. 1963 Feb;238:622–627. [PubMed] [Google Scholar]
  4. Chou P. Y., Fasman G. D. Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins. Biochemistry. 1974 Jan 15;13(2):211–222. doi: 10.1021/bi00699a001. [DOI] [PubMed] [Google Scholar]
  5. Chou P. Y., Fasman G. D. Prediction of protein conformation. Biochemistry. 1974 Jan 15;13(2):222–245. doi: 10.1021/bi00699a002. [DOI] [PubMed] [Google Scholar]
  6. Cohen C., Caspar D. L., Parry D. A., Lucas R. M. Tropomyosin crystal dynamics. Cold Spring Harb Symp Quant Biol. 1972;36:205–216. doi: 10.1101/sqb.1972.036.01.028. [DOI] [PubMed] [Google Scholar]
  7. Elliott A., Offer G. Shape and flexibility of the myosin molecule. J Mol Biol. 1978 Aug 25;123(4):505–519. doi: 10.1016/0022-2836(78)90204-8. [DOI] [PubMed] [Google Scholar]
  8. Harrington W. F. A mechanochemical mechanism for muscle contraction. Proc Natl Acad Sci U S A. 1971 Mar;68(3):685–689. doi: 10.1073/pnas.68.3.685. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Highsmith S., Kretzschmar K. M., O'Konski C. T., Morales M. F. Flexibility of myosin rod, light meromyosin, and myosin subfragment-2 in solution. Proc Natl Acad Sci U S A. 1977 Nov;74(11):4986–4990. doi: 10.1073/pnas.74.11.4986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Huxley H. E., Brown W. The low-angle x-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor. J Mol Biol. 1967 Dec 14;30(2):383–434. doi: 10.1016/s0022-2836(67)80046-9. [DOI] [PubMed] [Google Scholar]
  11. Kobayasi S., Totsuka T. Electric birefringence of myosin subfragments. Biochim Biophys Acta. 1975 Feb 17;376(2):375–385. doi: 10.1016/0005-2728(75)90029-8. [DOI] [PubMed] [Google Scholar]
  12. Laursen R. A. Solid-phase Edman degradation. An automatic peptide sequencer. Eur J Biochem. 1971 May 11;20(1):89–102. doi: 10.1111/j.1432-1033.1971.tb01366.x. [DOI] [PubMed] [Google Scholar]
  13. 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]
  14. Mendelson R. A., Morales M. F., Botts J. Segmental flexibility of the S-1 moiety of myosin. Biochemistry. 1973 Jun 5;12(12):2250–2255. doi: 10.1021/bi00736a011. [DOI] [PubMed] [Google Scholar]
  15. Nihel T., Mendelson R. A., Botts J. The site of force generation in muscle contraction as deduced from fluorescence polarization studies. Proc Natl Acad Sci U S A. 1974 Feb;71(2):274–277. doi: 10.1073/pnas.71.2.274. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Pepe F. A. The myosin filament. I. Structural organization from antibody staining observed in electron microscopy. J Mol Biol. 1967 Jul 28;27(2):203–225. doi: 10.1016/0022-2836(67)90016-2. [DOI] [PubMed] [Google Scholar]
  17. Smithies O., Gibson D., Fanning E. M., Goodfliesh R. M., Gilman J. G., Ballantyne D. L. Quantitative procedures for use with the Edman-Begg sequenator. Partial sequences of two unusual immunoglobulin light chains, Rzf and Sac. Biochemistry. 1971 Dec 21;10(26):4912–4921. doi: 10.1021/bi00802a013. [DOI] [PubMed] [Google Scholar]
  18. Starr R., Offer G. Polarity of the myosin molecule. J Mol Biol. 1973 Nov 25;81(1):17–31. doi: 10.1016/0022-2836(73)90244-1. [DOI] [PubMed] [Google Scholar]
  19. Sutoh K., Sutoh K., Karr T., Harrington W. F. Isolation and physico-chemical properties of a high molecular weight subfragment-2 of myosin. J Mol Biol. 1978 Nov 25;126(1):1–22. doi: 10.1016/0022-2836(78)90276-0. [DOI] [PubMed] [Google Scholar]
  20. Takahashi K. Topography of the myosin molecule as visualized by an improved negative staining method. J Biochem. 1978 Mar;83(3):905–908. doi: 10.1093/oxfordjournals.jbchem.a131988. [DOI] [PubMed] [Google Scholar]
  21. Thomas D. D., Seidel J. C., Hyde J. S., Gergely J. Motion of subfragment-1 in myosin and its supramolecular complexes: saturation transfer electron paramagnetic resonance. Proc Natl Acad Sci U S A. 1975 May;72(5):1729–1733. doi: 10.1073/pnas.72.5.1729. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
  23. 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]

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