Abstract
In order to understand the molecular mechanism of muscle movement or cell motility, identification and characterization of actin-binding sites on myosin head and myosin-binding sites on actin molecules are necessary. Elucidation of the correlation between the binding sites and the myosin ATPase reaction is also essential. We will discuss here an actin-binding site located around the reactive Cys(SH1)(705) on the myosin heavy chain and its role in the actomyosin ATPase reaction.
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References
Burke M, Reisler E (1977) Effect of nucleotide binding on the proximity of the essential sulfhydryl groups of myosin. Chemical probing of movement of residues during conformational transitions. Biochemistry 16: 5559–5563
Burke M, Rajasekharan N, Maruta S, Ikebe M (1990) A second consensus sequence of ATP-requiring proteins resides in the 21-kDa C-terminal segment of myosin subfragment-1. FEBS Lett. 262:185–188
Chaussepied P, Morales MF (1988) Modifying preselected sites on proteins: The stretch of residues 633–642 of the myosin heavy chain is part of the actin-binding site. Proc. Natl. Acad. Sci. USA 85:7471–7475
Elzinga M, Collins JH (1977) Amino acid sequence of a myosin fragment that contains SH-1, SH-2, and N-methylhistidine. Proc. Natl. Acad. Sci. USA 74: 4281–4284
Eto M, Suzuki R, Morita F, Kuwayama H, Nishi N, Tokura S (1990) Roles of the amino acid side chains in the actin-binding S-site of myosin heavy chain. J. Biochem. 108: 499–504
Garboczi DN, Fox AH, Gerring SL, Pedersen PL (1988) β-subunit of rat liver mitochondrial ATP synthase: cDNA cloning, amino acid sequence, expression in Escherichia coli, and structural relationship to adenylate kinase. Biochemistry 27: 553–560
Heil A, Muller G, Noda L, Pinder T, Schirmer H, Schirmer I, Von Zabern I (1974) The amino-acid sequence of porcine adenylate kinase from skeletal muscle. Eur. J. Biochem. 43: 131–144
Katoh T, Imae S, Morita F (1984) Binding of F-actin to a region between SH1 and SH2 groups of myosin subfragment-1 which may determine the high affinity of acto-subfragment-1 complex at rigor. J. Biochem. 95: 447–454
Katoh T, Morita F (1984) Interaction between myosin and F-actin. Correlation with actin-binding sites on subfragment-1. J. Biochem. 96:1223–1230
Katoh T, Katoh H, Morita F (1985) Actin-binding peptide obtained by the cyanogen bromide cleavage of the 20-kDa fragment of myosin subfragment-1. J. Biol. Chem. 260:6723–6727
Keane AM, Trayer IP, Levine BA, Zeugner C, Ruegg JC (1990) Peptide mimetics of an actin-binding site on myosin span two functional domains on actin. Nature 344:265–268
Lymn RW, Taylor EW (1971) Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry 10: 4617–4624
Morita F (1967) Interaction of heavy meromyosin with substrate I. Difference in ultraviolet absorption spectrum between heavy meromyosin and its Michaelis-Menten complex. J. Biol. Chem. 242:4501–4506
Morita F, Suzuki R, Nishi N, Tokura S (1988) Synthetic actin-binding peptides having the amino acid sequence around the reactive cysteinyl residues (SH1) of myosin heavy chain. Pept. Chem. 1987: 743–746
Mornet D, Pantel P, Audemard E, Kassab R (1979) The limited tryptic cleavage of chymotryptic S-1: An approach to the characterization of the actin site in myosin heads. Biochem. Biophys. Res. Commun. 89: 925–932
Pinkham JL, Platt T (1983) The nucleotide sequence of the rho gene of E. coli K-12. Nucleic Acids Research 11: 3531–3545
Reisler E, Burke M, Himmelfarb S, Harrington WF (1974) Spatial proximity of the two essential sulfhydryl groups of myosin. Biochemistry 13: 3837–3840
Reisler E, Burke M, Harrington WF (1977) Reactivity of essential thiols of myosin. Chemical probes of the activated state. Biochemistry 16: 5187–5191
Sutoh K (1983) Mapping of actin-binding sites on the heavy chain of myosin subfragment 1. Biochemistry 22: 1579–1585
Suzuki R, Nishi N, Tokura S, Morita F (1987) F-actin-binding synthetic heptapeptide having the amino acid sequence around the SH1 cysteinyl residue of myosin. J. Biol. Chem. 262: 11410–11412
Suzuki R, Morita F, Nishi N, Tokura S (1990) Inhibition of actomyosin subfragment 1 ATPase activity by analog peptides of the actin-binding site around the Cys(SH1) of myosin heavy chain. J. Biol. Chem. 265: 4939–4943
Tonomura Y (1986) Energy-transducing ATPases--structure and kinetics. Cambridge University Press, Cambridge London New York New Rochelle Melbourne Sydney
Walker JE, Saraste M, Runswick MJ, Gay NJ (1982) Distantly related sequences in the a- and b-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1: 945–951
Wells JA, Yount RG (1979) Active site trapping of nucleotides by crosslinking two sulfhydryls in myosin subfragment 1. Proc. Natl. Acad. Sci. USA 76: 4966–4970
Wells JA, Knoeber C, Sheldon MC, Werber MM, Yount RG (1980) Crosslinking of myosin subfragment-1. Nucleotide-enhanced modification by a variety of bifunctional reagents. J. Biol. Chem. 255: 11135–11140
Werber MM, Szent-Gyorgyi AG, Fasman GD (1972) Fluorescence studies on heavy meromyosin-substrate interaction. Biochemistry 11: 2872–2883
Yamamoto K, Sekine T (1979) Interaction of myosin subfragment-1 with actin II. Location of the actin binding site in a fragment of subfragment-1 heavy chain. J. Biochem. 86:1863–1868
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© 1991 Springer-Verlag Berlin Heidelberg
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Morita, F., Katoh, T., Suzuki, R., Isonishi, K., Hori, K., Eto, M. (1991). An Actin-Binding Site on Myosin. In: Rüegg, J.C. (eds) Peptides as Probes in Muscle Research. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-76409-7_5
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DOI: https://doi.org/10.1007/978-3-642-76409-7_5
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