Abstract
To begin to understand the nature of myosin subunit assembly, we determined the region of a vertebrate sarcomeric myosin heavy chain required for binding of light chain 1. We coexpressed in Escherichia coli segments of the rat alpha cardiac myosin heavy chain which spanned the carboxyl terminus of subfragment 1 and the amino terminus of subfragment 2 with a full-length rat cardiac myosin light chain 1. A 16 amino acid region of the myosin heavy chain (residues 792-808) was shown to be required for myosin light chain 1 binding in an immunoprecipitation assay.
Full Text
The Full Text of this article is available as a PDF (1,002.4 KB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Ashiba G., Szent-Györgyi A. G. Essential light chain exchange in scallop myosin. Biochemistry. 1985 Nov 5;24(23):6618–6623. doi: 10.1021/bi00344a048. [DOI] [PubMed] [Google Scholar]
- Bandman E. Myosin isoenzyme transitions in muscle development, maturation, and disease. Int Rev Cytol. 1985;97:97–131. doi: 10.1016/s0074-7696(08)62349-9. [DOI] [PubMed] [Google Scholar]
- Burke M., Sivaramakrishnam M., Kamalakannan V. On the mode of the alkali light chain association to the heavy chain of myosin subfragment 1. Evidence for the involvement of the carboxyl-terminal region of the heavy chain. Biochemistry. 1983 Jun 21;22(13):3046–3053. doi: 10.1021/bi00282a004. [DOI] [PubMed] [Google Scholar]
- Citi S., Kendrick-Jones J. Regulation of non-muscle myosin structure and function. Bioessays. 1987 Oct;7(4):155–159. doi: 10.1002/bies.950070404. [DOI] [PubMed] [Google Scholar]
- Eller M., Stedman H. H., Sylvester J. E., Fertels S. H., Rubinstein N. A., Kelly A. M., Sarkar S. Nucleotide sequence of full length human embryonic myosin heavy chain cDNA. Nucleic Acids Res. 1989 May 11;17(9):3591–3592. doi: 10.1093/nar/17.9.3591. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Flicker P. F., Wallimann T., Vibert P. Electron microscopy of scallop myosin. Location of regulatory light chains. J Mol Biol. 1983 Sep 25;169(3):723–741. doi: 10.1016/s0022-2836(83)80167-3. [DOI] [PubMed] [Google Scholar]
- Hammer J. A., 3rd, Bowers B., Paterson B. M., Korn E. D. Complete nucleotide sequence and deduced polypeptide sequence of a nonmuscle myosin heavy chain gene from Acanthamoeba: evidence of a hinge in the rodlike tail. J Cell Biol. 1987 Aug;105(2):913–925. doi: 10.1083/jcb.105.2.913. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hammer J. A., 3rd, Jung G., Korn E. D. Genetic evidence that Acanthamoeba myosin I is a true myosin. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4655–4659. doi: 10.1073/pnas.83.13.4655. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hardwicke P. M., Wallimann T., Szent-Györgyi A. G. Regulatory and essential light-chain interactions in scallop myosin. I. Protection of essential light-chain thiol groups by regulatory light-chains. J Mol Biol. 1982 Mar 25;156(1):141–152. doi: 10.1016/0022-2836(82)90463-6. [DOI] [PubMed] [Google Scholar]
- Henikoff S. Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing. Gene. 1984 Jun;28(3):351–359. doi: 10.1016/0378-1119(84)90153-7. [DOI] [PubMed] [Google Scholar]
- Kamm K. E., Stull J. T. The function of myosin and myosin light chain kinase phosphorylation in smooth muscle. Annu Rev Pharmacol Toxicol. 1985;25:593–620. doi: 10.1146/annurev.pa.25.040185.003113. [DOI] [PubMed] [Google Scholar]
- Karsch-Mizrachi I., Feghali R., Shows T. B., Leinwand L. A. Generation of a full-length human perinatal myosin heavy-chain-encoding cDNA. Gene. 1990 May 14;89(2):289–294. doi: 10.1016/0378-1119(90)90020-r. [DOI] [PubMed] [Google Scholar]
- Katoh T., Lowey S. Mapping myosin light chains by immunoelectron microscopy. Use of anti-fluorescyl antibodies as structural probes. J Cell Biol. 1989 Oct;109(4 Pt 1):1549–1560. doi: 10.1083/jcb.109.4.1549. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Korn E. D., Hammer J. A., 3rd Myosins of nonmuscle cells. Annu Rev Biophys Biophys Chem. 1988;17:23–45. doi: 10.1146/annurev.bb.17.060188.000323. [DOI] [PubMed] [Google Scholar]
- Kraft R., Bravo-Zehnder M., Taylor D. A., Leinwand L. A. Complete nucleotide sequence of full length cDNA for rat beta cardiac myosin heavy chain. Nucleic Acids Res. 1989 Sep 25;17(18):7529–7530. doi: 10.1093/nar/17.18.7529. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kraft R., Tardiff J., Krauter K. S., Leinwand L. A. Using mini-prep plasmid DNA for sequencing double stranded templates with Sequenase. Biotechniques. 1988 Jun;6(6):544-6, 549. [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Maita T., Hayashida M., Tanioka Y., Komine Y., Matsuda G. The primary structure of the myosin head. Proc Natl Acad Sci U S A. 1987 Jan;84(2):416–420. doi: 10.1073/pnas.84.2.416. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- McNally E. M., Buttrick P. M., Leinwand L. A. Ventricular myosin light chain 1 is developmentally regulated and does not change in hypertension. Nucleic Acids Res. 1989 Apr 11;17(7):2753–2767. doi: 10.1093/nar/17.7.2753. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McNally E. M., Gianola K. M., Leinwand L. A. Complete nucleotide sequence of full length cDNA for rat alpha cardiac myosin heavy chain. Nucleic Acids Res. 1989 Sep 25;17(18):7527–7528. doi: 10.1093/nar/17.18.7527. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McNally E. M., Goodwin E. B., Spudich J. A., Leinwand L. A. Coexpression and assembly of myosin heavy chain and myosin light chain in Escherichia coli. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7270–7273. doi: 10.1073/pnas.85.19.7270. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Miller J. B., Teal S. B., Stockdale F. E. Evolutionarily conserved sequences of striated muscle myosin heavy chain isoforms. Epitope mapping by cDNA expression. J Biol Chem. 1989 Aug 5;264(22):13122–13130. [PubMed] [Google Scholar]
- Mitchell E. J., Jakes R., Kendrick-Jones J. Localisation of light chain and actin binding sites on myosin. Eur J Biochem. 1986 Nov 17;161(1):25–35. doi: 10.1111/j.1432-1033.1986.tb10120.x. [DOI] [PubMed] [Google Scholar]
- Mitchell E. J., Karn J., Brown D. M., Newman A., Jakes R., Kendrick-Jones J. Regulatory and essential light-chain-binding sites in myosin heavy chain subfragment-1 mapped by site-directed mutagenesis. J Mol Biol. 1989 Jul 5;208(1):199–205. doi: 10.1016/0022-2836(89)90096-x. [DOI] [PubMed] [Google Scholar]
- Molina M. I., Kropp K. E., Gulick J., Robbins J. The sequence of an embryonic myosin heavy chain gene and isolation of its corresponding cDNA. J Biol Chem. 1987 May 15;262(14):6478–6488. [PubMed] [Google Scholar]
- Okamoto Y., Sekine T., Grammer J., Yount R. G. The essential light chains constitute part of the active site of smooth muscle myosin. Nature. 1986 Nov 6;324(6092):78–80. doi: 10.1038/324078a0. [DOI] [PubMed] [Google Scholar]
- Rimm D. L., Sinard J. H., Pollard T. D. Location of the head-tail junction of myosin. J Cell Biol. 1989 May;108(5):1783–1789. doi: 10.1083/jcb.108.5.1783. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Saez C. G., Myers J. C., Shows T. B., Leinwand L. A. Human nonmuscle myosin heavy chain mRNA: generation of diversity through alternative polyadenylylation. Proc Natl Acad Sci U S A. 1990 Feb;87(3):1164–1168. doi: 10.1073/pnas.87.3.1164. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sellers J. R., Harvey E. V. Localization of a light-chain binding site on smooth muscle myosin revealed by light-chain overlay of sodium dodecyl sulfate-polyacrylamide electrophoretic gels. J Biol Chem. 1984 Nov 25;259(22):14203–14207. [PubMed] [Google Scholar]
- Sivaramakrishnan M., Burke M. The free heavy chain of vertebrate skeletal myosin subfragment 1 shows full enzymatic activity. J Biol Chem. 1982 Jan 25;257(2):1102–1105. [PubMed] [Google Scholar]
- Strehler E. E., Strehler-Page M. A., Perriard J. C., Periasamy M., Nadal-Ginard B. Complete nucleotide and encoded amino acid sequence of a mammalian myosin heavy chain gene. Evidence against intron-dependent evolution of the rod. J Mol Biol. 1986 Aug 5;190(3):291–317. doi: 10.1016/0022-2836(86)90003-3. [DOI] [PubMed] [Google Scholar]
- Sweeney H. L., Kushmerick M. J., Mabuchi K., Sréter F. A., Gergely J. Myosin alkali light chain and heavy chain variations correlate with altered shortening velocity of isolated skeletal muscle fibers. J Biol Chem. 1988 Jun 25;263(18):9034–9039. [PubMed] [Google Scholar]
- Szentkiralyi E. M. Tryptic digestion of scallop S1: evidence for a complex between the two light-chains and a heavy-chain peptide. J Muscle Res Cell Motil. 1984 Apr;5(2):147–164. doi: 10.1007/BF00712153. [DOI] [PubMed] [Google Scholar]
- Tokunaga M., Suzuki M., Saeki K., Wakabayashi T. Position of the amino terminus of myosin light chain 1 and light chain 2 determined by electron microscopy with monoclonal antibody. J Mol Biol. 1987 Mar 20;194(2):245–255. doi: 10.1016/0022-2836(87)90372-x. [DOI] [PubMed] [Google Scholar]
- Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wagner P. D., Giniger E. Hydrolysis of ATP and reversible binding to F-actin by myosin heavy chains free of all light chains. Nature. 1981 Aug 6;292(5823):560–562. doi: 10.1038/292560a0. [DOI] [PubMed] [Google Scholar]
- Wallimann T., Szent-Györgyi A. G. An immunological approach to myosin light-chain function in thick filament linked regulation. 2. Effects of anti-scallop myosin light-chain antibodies. Possible regulatory role for the essential light chain. Biochemistry. 1981 Mar 3;20(5):1188–1197. doi: 10.1021/bi00508a021. [DOI] [PubMed] [Google Scholar]
- Warrick H. M., De Lozanne A., Leinwand L. A., Spudich J. A. Conserved protein domains in a myosin heavy chain gene from Dictyostelium discoideum. Proc Natl Acad Sci U S A. 1986 Dec;83(24):9433–9437. doi: 10.1073/pnas.83.24.9433. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yanagisawa M., Hamada Y., Katsuragawa Y., Imamura M., Mikawa T., Masaki T. Complete primary structure of vertebrate smooth muscle myosin heavy chain deduced from its complementary DNA sequence. Implications on topography and function of myosin. J Mol Biol. 1987 Nov 20;198(2):143–157. doi: 10.1016/0022-2836(87)90302-0. [DOI] [PubMed] [Google Scholar]
- Zaager S., Burke M. Subunit interactions of skeletal muscle myosin and myosin subfragment 1. Evidence for heavy chain-alkali light chain association-dissociation equilibrium. J Biol Chem. 1988 Jan 25;263(3):1513–1517. [PubMed] [Google Scholar]
- Zaager S., Burke M. Temperature and ionic strength dependence of the subunit interactions in vertebrate skeletal myosin. A comparison of the interaction between the alkali light and heavy chains of mammalian and avian myosin. J Biol Chem. 1988 Sep 25;263(27):13891–13895. [PubMed] [Google Scholar]
- de Boer H. A., Comstock L. J., Vasser M. The tac promoter: a functional hybrid derived from the trp and lac promoters. Proc Natl Acad Sci U S A. 1983 Jan;80(1):21–25. doi: 10.1073/pnas.80.1.21. [DOI] [PMC free article] [PubMed] [Google Scholar]