Effects of urea and guanidine hydrochloride on the sliding movement of actin filaments with ATP hydrolysis by myosin molecules

Journal of Biochemistry

Volumn 149, Issue 6, 2011, Pages 713-720

  Kumemoto, Ryusei ^a   Hosogoe, Yoshitsugu ^a   Nomura, Naoki ^a   Hatori, Kuniyuki ^a  

^a YAMAGATA UNIVERSITY   (Japan)

Author keywords

actomyosin; ATP hydrolysis; denaturant; hydration; motility

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATE; GLASS; GUANIDINE; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN HEAVY CHAIN; UREA;

ACTIN FILAMENT; ACTIN MYOSIN INTERACTION; ARTICLE; COMPLEX FORMATION; CONCENTRATION (PARAMETERS); CONCENTRATION RESPONSE; CONTROLLED STUDY; DENATURATION; ENZYME ACTIVATION; ENZYME ACTIVITY; HYDRATION; HYDROGEN BOND; HYDROLYSIS; PROTEIN QUATERNARY STRUCTURE; PROTEIN STABILITY; SURFACE PROPERTY;

ACTINS; ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; BIOCATALYSIS; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME ACTIVATION; GUANIDINE; HYDROGEN BONDING; HYDROLYSIS; MYOSINS; SPECTROMETRY, FLUORESCENCE; UREA;

EID: 79957800702     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvr020     Document Type: Article

References (25)

1. Highsmith, S., Duignan, K., Cooke, R., and Cohen, J. (1996) Osmotic pressure probe of actin-myosin hydration changes during ATP hydrolysis. Biophys. J. 70, 2830-2837 (Pubitemid 26175613)
2. Oplatka, A. (1994) The role of water in the mechanism of muscular contraction. FEBS Lett. 355, 1-3 (Pubitemid 24352090)
3. Kabir, S.R., Yokoyama, K., Mihashi, K., Kodama, T., and Suzuki, M. (2003) Hyper-mobile water is induced around actin filaments. Biophys. J. 85, 3154-3161 (Pubitemid 37345802)
4. Suzuki, M., Kabir, S.R., Siddique, M.S., Nazia, U.S., Miyazaki, T., and Kodama, T. (2004) Myosin-induced volume increase of the hyper-mobile water surrounding actin filaments. Biochem. Biophys. Res. Commun. 322, 340-346 (Pubitemid 39093875)
5. Kitamura, K., Tokunaga, M., Iwane, A.H., and Yanagida, T. (1999) A single myosin head moves along an actin filament with regular steps of 5.3 nanometres. Nature 397, 129-134 (Pubitemid 29050909)
6. Hua, L., Zhou, R., Thirumalai, D., and Berne, B.J. (2008) Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding. Proc. Natl Acad. Sci. USA 105, 16928-16933
7. Guo, F. and Friedman, J.M. (2009) Osmolyte-induced perturbations of hydrogen bonding between hydration layer waters: correlation with protein conformational changes. J. Phys. Chem. B 113, 16632-16642
8. Hayashi, Y., Katsumoto, Y., Omori, S., Kishii, N., and Yasuda, A. (2007) Liquid structure of the urea-water system studied by dielectric spectroscopy. J. Phys. Chem. B 111, 1076-1080
9. Panuszko, A., Bruzdziak, P., Zielkiewicz, J., Wyrzykowski, D., and Stangret, J. (2009) Effects of urea and trimethylamine-N-oxide on the properties of water and the secondary structure of hen egg white lysozyme. J. Phys. Chem. B 113, 14797-14809
10. Hierrezuelo, J.M., Molina-Bolvar, J.A., and Ruiz, C.C. (2009) On the urea action mechanism: a comparative study on the self-assembly of two sugar-based surfactants. J. Phys. Chem. B 113, 7178-7187
11. Soper, A.K., Castner, E.W., and Luzar, A. (2003) Impact of urea on water structure: a clue to its properties as a denaturant? Biophys. Chem. 105, 649-666 (Pubitemid 37123089)
12. O'Brien, E., Dima, R.I., Brooks, B., and Thirumalai, D. (2007) Interaction between hydrophobic and ionic solutes in aqueous guanidinium chloride and urea solutions: lessons for protein denaturation mechanism. J. Am. Chem. Soc. 129, 7346-7353 (Pubitemid 46980813)
13. Lim, W.K., Ro? sgen, J., and Englander, S.W. (2009) Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group. Proc. Natl Acad. Sci. USA 106, 2595-2600
14. Pardee, J.D. and Spudich, J.A. (1982) Purification of muscle actin. Methods Enzymol. 85, 164-181
15. Mardossian, S.S. and Lowey, S. (1982) Preparation of myosin and its sub-fragments from rabbit skeletal muscle. Methods Enzymol. 85, 55-71
16. Ohno, T. and Kodama, T. (1991) Kinetics of adenosine triphosphate hydrolysis by shortening myofibrils from rabbit psoas muscle. J. Physiol. 441, 685-702
17. Kuznetsova, I.M., Khaitlina, S.Y., Konditerov, S.N., Surin, A.M., and Turoverov, K.K. (1988) Changes of structure and intramolecular mobility in the course of actin denaturation. Biophys. Chem. 32, 73-78 (Pubitemid 19001125)
18. Ortiz-Costa, S., Sorenson, M.M., and Sola-Penna, M. (2008) Betaine protects urea-induced denaturation of myosin subfragment-1. FEBS J. 275, 3388-3396 (Pubitemid 351813550)
19. Mason, P., Brady, J.W., Neilson, G.W., and Dempsy, C.E. (2007) The interaction of guanidinium ions with a model peptide. Biophys. J. 93, L04-L06 (Pubitemid 47041643)
20. Greene, R.F. Jr and Pace, C.N. (1974) Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, alpha-chymotrypsin, and beta-lactoglobulin. J. Biol. Chem. 249, 5388-5393
21. Kawahara, K. and Tanford, C. (1966) Viscosity and density of aqueous solutions of urea and guanidine hydrochloride. J. Biol. Chem. 241, 3228-3232
22. Auton, M., Bolen, D.W., and Ro? sgen, J. (2008) Structural thermodynamics of protein preferential solvation: Osmolyte solvation of proteins, aminoacids, and peptides. Proteins 73, 802-813
23. Komatsu, H., Shigeoka, T., Ohno, T., Kaseda, K., Kanno, T., Matsumoto, Y., Suzuki, M., and Kodama, T. (2004) Modulation of actomyosin motor function by 1-hexanol. J. Muscle Res. Cell Motil. 25, 77-85 (Pubitemid 39023446)
24. Hatori, K., Honda, H., and Matsuno, K. (1995) ATP hydrolysis and sliding movement of actomyosin complex in the presence of ethanol. J. Biochem. 117, 264-266
25. Hatori, K., Honda, H., and Matsuno, K. (1996) ATP-dependent fluctuations of single actin filaments in vitro. Biophys. Chem. 58, 267-272 (Pubitemid 26066906)