PMID: 9428702Jan 15, 1998Paper

Interaction of F-actin with synthetic peptides spanning the loop region of human cardiac beta-myosin heavy chain containing Arg403

European Journal of Biochemistry
A BartegiA Fattoum

Abstract

The atomic model of the F-actin-myosin subfragment 1 complex (acto-S-1) from skeletal muscle suggests that the transition of the complex from a weakly to a strongly binding state, generating mechanical force during the contractile cycle, may involve the attachment of the upper 50-kDa subdomain of myosin subfragment 1 (S-1) to the interface between subdomains 1 and 3 of actin. For the human cardiac myosin, this putative interaction would take place at the ordered loop including Arg403 of the beta-heavy chain sequence, a residue whose mutation into Gln is known to elicit a severe hypertrophic cardiomyopathy caused by a decrease of the rate of the actomyosin ATPase activity. Moreover, in several nonmuscle myosins the replacement of a Glu residue within the homolog loop by Ser or Thr also results in the reduction of the actomyosin ATPase rate that is alleviated by phosphorylation. As an approach to the characterization of the unknown interaction properties of F-actin with this particular S-1 loop region, we have synthesized four 17-residue peptides corresponding to the sequence Gly398-Gly414 of the human beta-cardiac myosin. Three peptides included Arg403 (GG17) or Gln403 (GG17Q) or Ser409 (GG17S) and the fourth peptide (GG17sc) wa...Continue Reading

References

Jul 1, 1976·Archives of Biochemistry and Biophysics·R TakashiM F Morales
Aug 15, 1979·Journal of Molecular Biology·D D ThomasJ Gergely
Sep 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·H TowbinJ Gordon
Oct 15, 1992·European Journal of Biochemistry·C MéjeanY Benyamin
Feb 1, 1992·European Journal of Biochemistry·A HoumeidaC Roustan
Sep 1, 1991·Proceedings of the National Academy of Sciences of the United States of America·K SutohY Y Toyoshima
Sep 6, 1990·Nature·W KabschK C Holmes
Apr 15, 1988·Biochemical and Biophysical Research Communications·C MéjeanY Benyamin
Nov 1, 1989·Analytical Biochemistry·S C Gill, P H von Hippel
Oct 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·P Chaussepied, M F Morales
Mar 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·J C BulinskiS D Hauschka
Jan 1, 1995·Critical Reviews in Biochemistry and Molecular Biology·M Jackson, H H Mantsch
Dec 8, 1994·Nature·J A Spudich
Jun 1, 1993·The Journal of Clinical Investigation·G CudaN D Epstein
Dec 19, 1995·Proceedings of the National Academy of Sciences of the United States of America·H OnishiK Fujiwara
Jul 19, 1996·The Journal of Biological Chemistry·H Brzeska, E D Korn
Feb 7, 1997·Journal of Molecular Biology·A Orlova, E H Egelman
Feb 14, 1997·Journal of Molecular Biology·P VibertW Lehman

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Citations

Feb 19, 2000·Current Opinion in Cell Biology·N Volkmann, D Hanein
Oct 28, 1998·Proceedings of the National Academy of Sciences of the United States of America·C M YengoC L Berger
Oct 18, 2002·European Journal of Biochemistry·Valerie B PatchellBarry A Levine
Jan 1, 2004·Indian Journal of Clinical Biochemistry : IJCB·Sandhya MishraPraveen Sharma
Feb 8, 2005·The Journal of Biological Chemistry·Valerie B PatchellBarry A Levine

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