Literature DB >> 9826621

The influence of divalent cations on the dynamic properties of actin filaments: a spectroscopic study.

G Hild1, M Nyitrai, J Belágyi, B Somogyi.   

Abstract

The principal aim of this investigation was to study the change of the protein flexibility and/or conformational properties of actin filaments upon the replacement of Ca2+ by Mg2+. The temperature dependence of the fluorescence lifetime and the anisotropy decay of N-(iodoacetyl)-N'-(5-sulfo-1-naphthyl)ethylenediamine (IAEDANS) attached covalently to the Cys374 residue of actin were measured. Saturation transfer electron paramagnetic resonance (ST-EPR) experiments were also carried out using N-(1-oxyl-2,2,6, 6-tetramethyl-4-piperidinyl)-maleimide (MSL) attached to the same residue (Cys374). The Arrhenius analysis of the temperature dependence of the fluorescence lifetimes shows that for Mg-F-actin, both the activation energy (E*) and the frequency factor (A) are smaller than they are for Ca-F-actin. The longer rotational correlation times resolved in the fluorescence experiments are larger in the Mg2+-loaded form of the actin filament between 6 degreesC and 28 degreesC, but this difference becomes negligible above 28 degreesC. The results of saturation transfer electron paramagnetic resonance measurements on maleimide spin-labeled actin filaments indicate that the replacement of Ca2+ by Mg2+ induced a decrease of the mobility of the label on the sub-millisecond time scale. Based upon these results, we concluded that the filaments polymerized from Ca-actin are more flexible than the filaments of Mg-actin.

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Year:  1998        PMID: 9826621      PMCID: PMC1299972          DOI: 10.1016/S0006-3495(98)77742-2

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  37 in total

1.  Nanosecond pulsefluorometry in polarized light of G-actin-epsilon-ATP and F-actin-epsilon-ADP.

Authors:  K Mihashi; P Wahl
Journal:  FEBS Lett       Date:  1975-03-15       Impact factor: 4.124

2.  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.

Authors:  J A Spudich; S Watt
Journal:  J Biol Chem       Date:  1971-08-10       Impact factor: 5.157

3.  The measurement of actin concentration in solution: a comparison of methods.

Authors:  T W Houk; K Ue
Journal:  Anal Biochem       Date:  1974-11       Impact factor: 3.365

4.  Dynamics of fluorescence polarization in macromolecules.

Authors:  G G Belford; R L Belford; G Weber
Journal:  Proc Natl Acad Sci U S A       Date:  1972-06       Impact factor: 11.205

5.  Synthesis and characterization of two fluorescent sulfhydryl reagents.

Authors:  E N Hudson; G Weber
Journal:  Biochemistry       Date:  1973-10-09       Impact factor: 3.162

6.  Fluorescence spectroscopy of proteins.

Authors:  L Stryer
Journal:  Science       Date:  1968-11-01       Impact factor: 47.728

7.  Electron microscopic particle length of F-actin polymerized in vitro.

Authors:  M Kawamura; K Maruyama
Journal:  J Biochem       Date:  1970-03       Impact factor: 3.387

8.  Dynamic study of F-actin by quasielastic scattering of laser light.

Authors:  S Fujime; S Ishiwata
Journal:  J Mol Biol       Date:  1971-11-28       Impact factor: 5.469

9.  Nanosecond pulse fluorometry in polarized light of dansyl-L-cysteine linked to a unique SH group of F-actin; the influence of regulatory proteins and myosin moiety.

Authors:  P Wahl; K Mihashi; J C Auchet
Journal:  FEBS Lett       Date:  1975-12-01       Impact factor: 4.124

10.  Spectroscopic study of conformational changes in subdomain 1 of G-actin: influence of divalent cations.

Authors:  M Nyitrai; G Hild; J Belágyi; B Somogyi
Journal:  Biophys J       Date:  1997-10       Impact factor: 4.033

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  6 in total

1.  Conformational changes in actin filaments induced by formin binding to the barbed end.

Authors:  Gábor Papp; Beáta Bugyi; Zoltán Ujfalusi; Szilvia Barkó; Gábor Hild; Béla Somogyi; Miklós Nyitrai
Journal:  Biophys J       Date:  2006-07-07       Impact factor: 4.033

2.  EFFECT OF PHALLOIDIN ON FILAMENTS POLYMERIZED FROM HEART MUSCLE ADP-ACTIN MONOMERS.

Authors:  Andrea Vig; Réka Dudás; Tünde Kupi; J Orbán; G Hild; D Lőrinczy; M Nyitrai
Journal:  J Therm Anal Calorim       Date:  2009-03-20       Impact factor: 4.626

3.  Myosin and tropomyosin stabilize the conformation of formin-nucleated actin filaments.

Authors:  Zoltán Ujfalusi; Mihály Kovács; Nikolett T Nagy; Szilvia Barkó; Gábor Hild; András Lukács; Miklós Nyitrai; Beáta Bugyi
Journal:  J Biol Chem       Date:  2012-06-29       Impact factor: 5.157

Review 4.  Conformational dynamics of actin: effectors and implications for biological function.

Authors:  Gábor Hild; Beáta Bugyi; Miklós Nyitrai
Journal:  Cytoskeleton (Hoboken)       Date:  2010-10

5.  Rotational motion of rhodamine 6G tethered to actin through oligo(ethylene glycol) linkers studied by frequency-domain fluorescence anisotropy.

Authors:  Tetsuichi Wazawa; Nobuyuki Morimoto; Takeharu Nagai; Makoto Suzuki
Journal:  Biophys Physicobiol       Date:  2015-12-02

6.  Cardiac leiomodin2 binds to the sides of actin filaments and regulates the ATPase activity of myosin.

Authors:  Dávid Szatmári; Beáta Bugyi; Zoltán Ujfalusi; László Grama; Réka Dudás; Miklós Nyitrai
Journal:  PLoS One       Date:  2017-10-12       Impact factor: 3.240

  6 in total

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