Open accessthermal denaturation and aggregation of myosin subfragment 1 isoforms with different essential light chains

International Journal of Molecular Sciences

Volumn 11, Issue 11, 2010, Pages 4194-4226

  Markov, Denis I ^a   Zubov, Eugene O ^a   Nikolaeva, Olga P ^b   Kurganov, Boris I ^a   Levitsky, Dmitrii I ^a,b  

^a BACH INSTITUTE OF BIOCHEMISTRY   (Russian Federation)

^b MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

Differential scanning calorimetry; Dynamic light scattering; Heat induced aggregation; Myosin subfragment 1; Thermal denaturation

Indexed keywords

MYOSIN LIGHT CHAIN; MYOSIN SUBFRAGMENT 1; ISOPROTEIN; MYOSIN SUBFRAGMENT;

ARTICLE; CONTROLLED STUDY; DENATURATION; DIFFERENTIAL SCANNING CALORIMETRY; IONIC STRENGTH; LIGHT SCATTERING; MUSCLE CELL; NONHUMAN; PROTEIN AGGREGATION; PROTEIN DOMAIN; PROTEIN STRUCTURE; RABBIT; TEMPERATURE DEPENDENCE; ANIMAL; BIOLOGICAL MODEL; CHEMISTRY; DYNAMIC LIGHT SCATTERING; HEAT-INDUCED AGGREGATION; HUMAN; POLYMERIZATION; PROTEIN DENATURATION; PROTEIN STABILITY; TEMPERATURE; THERMAL DENATURATION;

DIFFERENTIAL SCANNING CALORIMETRY; DYNAMIC LIGHT SCATTERING; HEAT-INDUCED AGGREGATION; MYOSIN SUBFRAGMENT 1; THERMAL DENATURATION;

ANIMALS; HUMANS; MODELS, BIOLOGICAL; MYOSIN LIGHT CHAINS; MYOSIN SUBFRAGMENTS; POLYMERIZATION; PROTEIN DENATURATION; PROTEIN ISOFORMS; PROTEIN STABILITY; TEMPERATURE;

EID: 78650994573     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms11114194     Document Type: Article

References (40)

1. Rayment, I.; Rypniewski, W.P.; Schmidt-Base, K.; Smith, R.; Tomchick, D.R.; Benning, M.M.; Winkelmann, D.A.; Wesenberg, G.; Holden, H.M. Three-dimensional structure of myosin subfragment 1: a molecular motor. Science 1993, 261, 50-58.
2. Rayment, I. The structural basis of the myosin ATPase activity. J. Biol. Chem. 1996,271, 15850-15853.
3. Uyeda, T.Q.; Abramson, P.D.; Spudich, J.A. The neck region of the myosin motor domain acts as a lever arm to generate movement. Proc. Natl. Acad. Sci. USA 1996, 93, 4459-4464.
4. Weeds, A.G.; Taylor, R.S. Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin. Nature 1975, 257, 54-56.
5. Frank, G.; Weeds, A.G. The amino-acid sequence of the alkali light chains of rabbit skeletal muscle myosin. Eur. J. Biochem. 1974, 44, 317-334.
6. Wagner, P.D.; Slayter, C.S.; Pope, B.; Weeds, A.G. Studies on the actin activation of myosin subfragment-1 isoenzymes and the role of the myosin light chains. Eur. J. Biochem. 1979,99, 385-394.
7. Chalovich, J.M.; Stein, L.A.; Greene, L.E.; Eisenberg, E. Interaction of isozymes of myosin subfragment 1 with actin: effect of ionic strength and nucleotide. Biochemistry 1984, 23, 4885-4889.
8. Sutoh, K. Identification of myosin-binding sites on the actin sequence. Biochemistry 1982, 21, 3654-3661.
9. Trayer, I.P.; Trayer, H.R.; Levine, B.A. Evidence that the N-terminal region of A1-light chain of myosin interacts directly with the C-terminal region of actin. A proton magnetic resonance study. Eur. J. Biochem. 1987, 164, 259-266.
10. Hayashibara, T.; Miyanishi, T. Binding of the amino-terminal region of myosin alkali 1 light chain to actin and its effect on actin-myosin interaction. Biochemistry 1994, 33, 12821-12827.
11. Andreev, O.A.; Saraswat, L.D.; Lowey, S.; Slaughter, C.; Borejdo, J. Interaction of the N-terminus of chicken skeletal essential light chain 1 with F-actin. Biochemistry 1999, 38, 2480-2485.
12. Pliszka, B.; Redowicz, M.J.; Stepkowski, D. Interaction of the N-terminal part of the A1 essential light chain with the myosin heavy chain. Biochem. Biophys. Res. Commun. 2001, 281, 924-928.
13. Borejdo, J.; Ushakov, D.S.; Moreland, R.; Akopova, I.; Reshetnyak, Y.; Saraswat, L.D.; Kamm, K.; Lowey, S. The power stroke causes changes in the orientation and mobility of the termini of essential light chain 1 of myosin. Biochemistry 2001, 40, 3796-3803.
14. Lowey, S.; Saraswat, L.D.; Liu, H.; Volkmann, N.; Hanein, D. Evidence for an interaction between the SH3 domain and the N-terminal extension of the essential light chain in class II myosins. J. Mol. Biol. 2007, 371, 902-913.
15. Mrakovcic-Zenic, A.; Oriol-Audit, C.; Reisler, E. On the alkali light chains of vertebrate skeletal myosin. Nucleotide binding and salt-induced conformational changes. Eur. J. Biochem. 1981, 115, 565-570.
16. Levitsky, D.I.; Nikolaeva, O.P.; Vedenkina, N.S.; Shnyrov, V.L.; Golitsina, N.L.; Khvorov, N.V.; Permyakov, E.A.; Poglazov, B.F. The effect of alkali light chains on the thermal stability of myosin subfragment 1. Biomed. Sci. 1991, 2, 140-146.
17. Abillon, E.; Bremier, L.; Cardinaud, R. Conformational calculations on the Ala14-Pro27 LC1 segment of rabbit skeletal myosin. Biochim. Biophys. Acta 1990, 1037, 394-400.
18. Kurganov, B.I.; Lyubarev, A.E.; Sanchez-Ruiz, J.M.; Shnyrov, V.L. Analysis of differential scanning calorimetry data for proteins. Criteria of validity of one-step mechanism of irreversible protein denaturation. Biophys. Chem. 1997, 69, 125-135.
19. Levitsky, D.I.; Khvorov, N.V.; Shnyrov, V.L.; Vedenkina, N.S.; Permyakov, E.A.; Poglazov, B.F. Domain structure of myosin subfragment-1. Selective denaturation of the 50 kDa segment. FEBS Lett. 1990, 264, 176-178.
20. Levitsky, D.I.; Shnyrov, V.L.; Khvorov, N.V.; Bukatina, A.E.; Vedenkina, N.S.; Permyakov, E.A.; Nikolaeva, O.P.; Poglazov, B.F. Effects of nucleotide binding on thermal transitions and domain structure of myosin subfragment 1. Eur. J. Biochem. 1992, 209, 829-835.
21. Levitsky, D.I. Domain Structure of the Myosin Head. In Soviet Scientific Reviews. Section D: Physico-Chemical Biology; Harwood Academic Publishers GmbH: Newark, NJ, USA, 1994; Volume 12, pp. 1-53.
22. Tong, S.W.; Elzinga, M. Amino acid sequence of rabbit skeletal muscle myosin. 50-kDa fragment of the heavy chain. J. Biol. Chem. 1990, 265, 4893-4901.
23. Permyakov, E.A.; Burstein, E.A. Some aspects of studies of thermal transitions in proteins by means of their intrinsic fluorescence. Biophys. Chem. 1984, 19, 265-271.
24. Kuznetsova, I.M.; Stepanenko, O.V.; Stepanenko, O.V.; Povarova, O.I.; Biktashev, A.G.; Verkhusha, V.V.; Shavlovsky, M.M.; Turoverov, K.K. The place of inactivated actin and its kinetic predecessor in actin folding-unfolding. Biochemistry 2002, 41, 13127-13132.
25. Khanova, H.A.; Markossian, K.A.; Kurganov, B.I.; Samoilov, A.M.; Kleimenov, S.Yu.; Levitsky, D.I.; Yudin, I.K.; Timofeeva, A.C.; Muranov, K.O.; Ostrovsky, M.A. Mechanism of chaperone-like activity. Suppression of thermal aggregation of beta-L-crystallin by alpha-crystallin. Biochemistry 2005,44,15480-15487.
26. Markossian, K.A.; Khanova, H.A.; Kleimenov, S.Yu.; Levitsky, D.I.; Chebotareva, N.A.; Asryants, R.A.; Muronetz, V.I.; Saso, L.; Yudin, I.K.; Kurganov, B.I. Mechanism of thermal aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 2006, 45, 13375-13384.
27. Markossian, K.A.; Yudin, I.K.; Kurganov, B.I. Mechanism of suppression of protein aggregation by alpha-crystallin. Int. J. Mol. Sci. 2009, 10, 1314-1345.
28. Trayer, H.R.; Trayer, I.P. Fluorescence resonance energy transfer within the complex formed by actin and myosin subfragment 1. Comparison between weakly and strongly attached states. Biochemistry 1988, 27, 5718-5727.
29. Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
30. Nikolaeva, O.P.; Orlov, V.N.; Bobkov, A.A.; Levitsky, D.I. Differential scanning calorimetric study of myosin subfragment 1 with tryptic cleavage at the N-terminal region of the heavy chain. Eur. J. Biochem. 2002, 269, 5678-5688.
31. Shakirova, L.I.; Mikhailova, V.V.; Siletskaya, E.I.; Timofeev, V.P.; Levitsky, D.I. Nucleotide-induced and actin-induced structural changes in SH1-SH2-modified myosin subfragment 1. J. Muscle Res. Cell Motil. 2007, 28, 67-78.
32. Markov, D.I.; Pivovarova, A.V.; Chernik, I.S.; Gusev, N.B.; Levitsky, D.I. Small heat shock protein Hsp27 protects myosin S1 from heat-induced aggregation, but not from thermal denaturation and ATPase inactivation. FEBS Lett. 2008, 582, 1407-1412.
33. Kremneva, E.; Nikolaeva, O.; Maytum, R.; Arutyunyan, A.M.; Kleimenov, S.Yu.; Geeves, M.A.; Levitsky, D.I. Thermal unfolding of smooth muscle and non-muscle tropomyosin alpha-homodimers with alternatively spliced exons. FEBS J. 2006, 273, 588-600.
34. Lopez Mayorga, O.; Freire, E. Dynamic analysis of differential scanning calorimetry data. Biophys. Chem. 1987, 27, 87-96.
35. Filimonov, V.V.; Potekhin, S.A.; Matveev, S.V.; Privalov, P.L. Thermodynamic analysis of scanning microcalorimetry data. 1. Algorithms for deconvolution of heat absorption curves. Mol. Biol. (Mosk) 1982, 16, 551-562 (in Russian).
36. Turoverov, K.K.; Haitlina, S.Yu.; Pinaev, G.P. Ultra-violet fluorescence of actin. Determination of native actin content in actin preparations. FEBS Lett. 1976, 62, 4-6.
37. Turoverov, K.K.; Kuznetsova, I.M. Intrinsic fluorescence of actin. J. Fluoresc. 2003, 13, 41-57.
38. Staiano, M.; Scognamiglio, V.; Rossi, M.; D'Auria, S.; Stepanenko, O.V.; Kuznetsova, I.M.; Turoverov, K.K. Unfolding and refolding of the glutamine-binding protein from Escherichia coli and its complex with glutamine induced by guanidine hydrochloride. Biochemistry 2005, 44, 5625-5633.
39. Panusz, H.T.; Graczyk, G.; Wilmanska, D.; Skarzynski, J. Analysis of orthophosphate-pyrophosphate mixtures resulting from weak pyrophosphatase activities. Anal. Biochem. 1970, 35, 494-504.
40. Markov, D.I.; Nikolaeva, O.P.; Levitsky, D.I. Effects of myosin "essential" light chain A1 on aggregation properties of the myosin head. Acta Naturae 2010, 2, No. 2(5), 77-81.