Interaction of formin FH2 with skeletal muscle actin. EPR and DSC studies

European Biophysics Journal

Volumn 42, Issue 10, 2013, Pages 757-765

  Kupi, Tünde ^a   Gróf, Pál ^b   Nyitrai, Miklós ^a,c,d   Belágyi, József ^a  

^a UNIVERSITY OF PÉCS   (Hungary)

^b SEMMELWEIS UNIVERSITY OF MEDICINE   (Hungary)

^c UNIVERSITY OF PÉCS   (Hungary)

^d INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

Author keywords

Actin; Cytoskeleton; Electron paramagnetic resonance; Formin; Maleimido TEMPO; Protein conformation

Indexed keywords

ALPHA ACTIN; CYTOSKELETON PROTEIN; DIMER; FLUORESCENT DYE; FORMIN HOMOLOGY 2 DOMAIN; MALEIMIDE; MONOMER; THIOL GROUP; UNCLASSIFIED DRUG;

ACTIN POLYMERIZATION; ARTICLE; CONFORMATIONAL TRANSITION; DIFFERENTIAL SCANNING CALORIMETRY; ELECTRON SPIN RESONANCE; MOLECULAR MECHANICS; MOLECULAR PROBE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; SKELETAL MUSCLE; TEMPERATURE; TEMPERATURE DEPENDENCE;

EUKARYOTA;

ACTINS; ANIMALS; CALORIMETRY, DIFFERENTIAL SCANNING; ELECTRON SPIN RESONANCE SPECTROSCOPY; FETAL PROTEINS; HOT TEMPERATURE; MICROFILAMENT PROTEINS; MUSCLE, SKELETAL; NUCLEAR PROTEINS; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY;

EID: 84896692439     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-013-0922-0     Document Type: Article

References (30)

1. Belagyi J, Grof P (1983) Rotational motion of actin monomer at low and high salt concentration. Europ J Biochem 130:353-358
2. Bruylants G, Wouters J, Michaux C (2005) Differential scanning calorimetry in life science: thermodynamics, stability, molecular recognition and application in drug design. Curr Med Chem 12:2011-2020
3. Bugyi B, Papp G, Hild G, Lorinczy D, Nevalainen EM, Lappalainen P, Somogyi B, Nyitrai M (2006) Formins regulate actin filament flexibility through long range allosteric interactions. J Biol Chem 281:10727-10736
4. Burley RW, Seidel JC, Gergely J (1971) The stoichiometry of the reaction of the spin labeling of F-actin and the effect of orientation of spin-labeled F-actin filaments. Arch Biochem Biophys 146:597-602
5. Criddle AH, Geeves MA, Jeffries T (1985) The use of actin labelled with N-(1-pyrenyl) iodoacetamide to study the interaction of actin with myosin sub-fragments and troponin/tropomyosin. Biochem J 232:343-349
6. Goldman SA, Bruno GV, Freed JH (1972) Estimating slow-motional rotational correlation times for nitroxides by electron spin resonance. J Phys Chem 76:1858-1860
7. Hild G, Bugyi B, Nyitrai M (2010) Conformational dynamics of actin: effectors and implications for biological function. Cytoskeleton (Hoboken) 67:609-629
8. Houk TW Jr, Ue K (1974) The measurement of actin concentration in solution: a comparison of methods. Anal Biochem 62:66-74
9. Jones RH, Molitoris BA (1984) A statistical method for determining the breakpoint of two lines. Anal Biochem 141:287-290
10. Kouyama T, Mihashi K (1981) Fluorimetry study of N-(1-pyrenyl) iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. Eur J Biochem 114:33-38
11. Kupi T, Grof P, Nyitrai M, Belagyi J (2009) The uncoupling of the effects of formins on the local and global dynamics of actin filaments. Biophys J 96:2901-2911
12. Lappalainen P (2007) Actin-monomer-binding proteins. In: Lappalainen P (ed). Springer, New York
13. Moseley JB, Sagot I, Manning AL, Xu Y, Eck MJPD, Goode BL (2004) A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin. Mol Biol Cell 15:896-907
14. Mossakowska M, Belagyi J, Strzelecka-Golaszewska H (1988) An EPR study of the rotational dynamics of actins from striated and smooth muscle and their complexes with heavy meromyosin. Eur J Biochem 175:557-564
15. Nyitrai M, Hild G, Belagyi J, Somogyi B (1997) Spectroscopic study of conformational changes in subdomain 1 of G-actin: influence of divalent cations. Biophys J 73:2023-2032
16. Pantaloni D, Le Clainche C, Carlier MF (2001) Mechanism of actin-based motility. Science 292:1502-1506
17. Papp G, Bugyi B, Ujfalusi Z, Barko S, Hild G, Somogyi B, Nyitrai M (2006) Conformational changes in actin filaments induced by formin binding to the barbed end. Biophys J 91:2564-2572
18. Pollard TD, Borisy GG (2003) Cellular motility driven by assembly and disassembly of actin filaments. Cell 112:453-465
19. Pollard TD, Blanchoin L, Mullins RD (2000) Molecular mechanisms controlling actin filament dynamics in non-muscle cells. Annu Rev Biophys Biomol Struct 29:545-576
20. Privalov PL, Potekhin SA (1986) Scanning micro calorimetry in studying temperature-induced changes in proteins. Meth Enzym 131:4-51
21. Sanchez-Ruiz JM (1992) Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry. Biophys J 61:921-935
22. Sanchez-Ruiz JM, Lopez-Lacomba JL, Cortijo M, Mateo PL (1988a) Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin. Biochemistry 27:1648-1652
23. Sanchez-Ruiz JM, Lopez-Lacomba JL, Mateo PL, Vilanova M, Serra MA, Aviles FX (1988b) Analysis of the thermal unfolding of porcine procarboxypeptidase A and its functional pieces by differential scanning calorimetry. Eur J Biochem 176:225-230
24. Shimada A, Nyitrai M, Vetter IR, Kuhlmann D, Bugyi B, Narumiya S, Geeves MA, Wittinghofer A (2004) The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization. Mol Cell 13:511-522
25. Spudich JA, Watt S (1971) The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem 246:4866-4871
26. Thomas DD, Seidel JC, Gergely J, Hyde JS (1975) The quantitative measurement of rotational motion of the subfragment-1 region of myosin by saturation transfer epr spectroscopy. J Supramol Struct 3:376-390
27. Thomas DD, Seidel JC, Gergely J (1979) Rotational dynamics of spin-labeled F-actin in the sub-millisecond time range. J Mol Biol 132:257-273
28. Tobacman LS, Korn ED (1983) The kinetics of actin nucleation and polymerization. J Biol Chem 258:3207-3214
29. Xu Y, Moseley JB, Sagot I, Poy F, Pellman D, Goode BLaE MJ (2005) Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture. Cell 116:711-723
30. Zigmond SH (2004) Formin-induced nucleation of actin filaments. Curr Opin Cell Biol 16:99-105