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
. 1987 Jan;84(2):416–420. doi: 10.1073/pnas.84.2.416

The primary structure of the myosin head.

T Maita, M Hayashida, Y Tanioka, Y Komine, G Matsuda
PMCID: PMC304218  PMID: 3467365

Abstract

The sequence of the NH2-terminal 808 amino acid residues of chicken pectoralis muscle myosin head was determined. Three characteristic 20-, 23-, and 50-kDa fragments were isolated from a digest of myosin subfragment 1 (S1) by gel filtration on a Sephadex G-100 column in the presence of 5 M guanidine hydrochloride, followed by anion-exchange chromatography on a QAE-Sephadex A-50 column in the presence of 8 M urea. The fragments were sequenced completely by conventional methods. Peptides overlapping the 23- and 50-kDa fragments and also overlapping the 50- and 20-kDa fragments were obtained by cleaving S1 with cyanogen bromide. Comparison of the 23-kDa and 50-kDa sequences with that of the overlapping peptide indicated that no additional amino acid exists between the 23- and 50-kDa fragments and that 5 amino acids exist between the 50- and 20-kDa fragments of S1. Methylated amino acid residues were found at four positions: epsilon-N-monomethyllysine at position 35, epsilon-N-trimethyllysine residues at 130 and 550, and 3-N-methylhistidine at 754.

Full text

PDF
419

Images in this article

417Image
on p.417

Selected References

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

  1. Applegate D., Reisler E. Protease-sensitive regions in myosin subfragment 1. Proc Natl Acad Sci U S A. 1983 Dec;80(23):7109–7112. doi: 10.1073/pnas.80.23.7109. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bálint M., Wolf I., Tarcsafalvi A., Gergely J., Sréter F. A. Location of SH-1 and SH-2 in the heavy chain segment of heavy meromyosin. Arch Biochem Biophys. 1978 Oct;190(2):793–799. doi: 10.1016/0003-9861(78)90339-9. [DOI] [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. Kropp K., Gulick J., Robbins J. A canonical sequence organization at the 5'-end of the myosin heavy chain genes. J Biol Chem. 1986 May 15;261(14):6613–6618. [PubMed] [Google Scholar]
  5. MUELLER H., PERRY S. V. The degradation of heavy meromyosin by trypsin. Biochem J. 1962 Dec;85:431–439. doi: 10.1042/bj0850431. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Maita T., Morokuma K., Matsuda G. Amino acid sequences of the tryptic peptides from carboxymethylated L-asparaginase from Escherichia coli. Hoppe Seylers Z Physiol Chem. 1979 Oct;360(10):1483–1495. doi: 10.1515/bchm2.1979.360.2.1483. [DOI] [PubMed] [Google Scholar]
  7. Maita T., Umegane T., Kato Y., Matsuda G. Amino-acid sequence of the L-1 light chain of chicken cardiac-muscle myosin. Eur J Biochem. 1980 Jun;107(2):565–575. doi: 10.1111/j.1432-1033.1980.tb06064.x. [DOI] [PubMed] [Google Scholar]
  8. Maita T., Umegane T., Matsuda G. Amino-acid sequence of the L-4 light chain of chicken skeletal-muscle myosin. Eur J Biochem. 1981;114(1):45–49. doi: 10.1111/j.1432-1033.1981.tb06169.x. [DOI] [PubMed] [Google Scholar]
  9. Matsuda G., Suzuyama Y., Maita T., Umegane T. The L-2 light chain of chicken skeletal muscle myosin. FEBS Lett. 1977 Dec 1;84(1):53–56. doi: 10.1016/0014-5793(77)81055-7. [DOI] [PubMed] [Google Scholar]
  10. Mornet D., Ue K., Morales M. F. Proteolysis and the domain organization of myosin subfragment 1. Proc Natl Acad Sci U S A. 1984 Feb;81(3):736–739. doi: 10.1073/pnas.81.3.736. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Okamoto Y., Yount R. G. Identification of an active site peptide of skeletal myosin after photoaffinity labeling with N-(4-azido-2-nitrophenyl)-2-aminoethyl diphosphate. Proc Natl Acad Sci U S A. 1985 Mar;82(6):1575–1579. doi: 10.1073/pnas.82.6.1575. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Rayment I., Winkelmann D. A. Crystallization of myosin subfragment 1. Proc Natl Acad Sci U S A. 1984 Jul;81(14):4378–4380. doi: 10.1073/pnas.81.14.4378. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Robbins J., Horan T., Gulick J., Kropp K. The chicken myosin heavy chain family. J Biol Chem. 1986 May 15;261(14):6606–6612. [PubMed] [Google Scholar]
  14. Tong S. W., Elzinga M. The sequence of the NH2-terminal 204-residue fragment of the heavy chain of rabbit skeletal muscle myosin. J Biol Chem. 1983 Nov 10;258(21):13100–13110. [PubMed] [Google Scholar]
  15. Tsunasawa S., Narita K. Micro-identification of amino-terminal acetylamino acids in proteins. J Biochem. 1982 Sep;92(3):607–613. doi: 10.1093/oxfordjournals.jbchem.a133971. [DOI] [PubMed] [Google Scholar]
  16. Umegane T., Maita T., Matsuda G. Amino-acid sequence of the L-1 light chain of chicken fast skeletal-muscle myosin. Hoppe Seylers Z Physiol Chem. 1982 Nov;363(11):1321–1330. doi: 10.1515/bchm2.1982.363.2.1321. [DOI] [PubMed] [Google Scholar]
  17. 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]
  18. Weeds A. G., Taylor R. S. Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin. Nature. 1975 Sep 4;257(5521):54–56. doi: 10.1038/257054a0. [DOI] [PubMed] [Google Scholar]
  19. Winkelmann D. A., Mekeel H., Rayment I. Packing analysis of crystalline myosin subfragment-1. Implications for the size and shape of the myosin head. J Mol Biol. 1985 Feb 20;181(4):487–501. doi: 10.1016/0022-2836(85)90422-x. [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