Solution structure and dynamics of ADF/cofilin from Leishmania donovani

Journal of Structural Biology

Volumn 172, Issue 3, 2010, Pages 219-224

  Pathak, Prem Prakash ^a   Pulavarti, S V S R Krishna ^a   Jain, Anupam ^a   Sahasrabuddhe, Amogh Anant ^a   Gupta, Chhitar Mal ^a   Arora, Ashish ^a  

^a CENTRAL DRUG RESEARCH INSTITUTE   (India)

Author keywords

ADF cofilin; Backbone dynamics; Leishmania donovani; NMR; Protein structure

Indexed keywords

ADENOSINE DIPHOSPHATE; COFILIN; F ACTIN; G ACTIN; NITROGEN 15;

ALPHA HELIX; ARTICLE; BETA SHEET; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; LEISHMANIA DONOVANI; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE; STOICHIOMETRY;

ACTIN DEPOLYMERIZING FACTORS; ACTINS; ANIMALS; CALORIMETRY; LEISHMANIA DONOVANI; MAGNETIC RESONANCE SPECTROSCOPY; MUSCLE, SKELETAL; PROTOZOAN PROTEINS; RABBITS;

LEISHMANIA DONOVANI; ORYCTOLAGUS CUNICULUS;

EID: 77958470449     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2010.07.001     Document Type: Article

References (39)

1. Abe H., Obinata T. J. Biochemistry 1989, 106:172-180.
2. Ashworth S.L., Southgate E.L., Sandoval R.M., Meberg P.J., Bamburg J.R., Molitoris B.A. ADF/cofilin mediates actin cytoskeletal alterations in LLC-PK cells during ATP depletion. Am. J. Physiol. Renal. 2003, 284:F852-F862.
3. Berman H.M., Battistuz T., Bhat T.N., Bluhm W.F., Bourne P.E., Burkhardt K., Feng Z., Gilliland G.L., Iype L., Jain S., et al. The protein data bank. Acta Crystallogr. D 2002, 58:899-907.
4. Brunger A.T., Adams P.D., Clore G.M., Delano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.S., Kuszewski J., Nilges M., Pannu N.S., Read R.J., Rice L.M., Simonson T., Warren G.L. Crystallography and NMR system (CNS): a new software suite for macromolecular structure determination. Acta Crystallogr. 1998, 54:905-921.
5. Carlier M.F., Laurent V., Santolini J., Melki R., Didry D., Xia G.-X., Hong Y., Chua N.-H., Pantaloni D. Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. J. Cell. Biol. 1997, 136:1307-1322.
6. 15N nuclear magnetic relaxation of proteins. J. Am. Chem. Soc. 1990, 112:4989-4991.
7. Dai H., Huang W., Xu J., Yao B., Xiong S., Ding H., Tang Y., Liu H., Wu J., Shi Y. Binding model of human coactosin-like protein with filament actin revealed by mutagenesis. Biochim. Biophys. Acta 2006, 1764:1688-1700.
8. Guntert P., Mumenthaler C., Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 1997, 271:283-298.
9. Holm L., Kaariainen S., Rosenstrom P., Schenkel A. Searching protein structure databases with DaliLite v.3. Bioinformatics 2008, 24:2780-2781.
10. Jung J.W., Yee A., Wu B., Arrowsmith C.H., Lee W. Solution structure of YKR049C, a putative redox protein from Saccharomyces cerevisiae. J. Biochem. Mol. Biol. 2005, 38:550-554.
11. Kapoor P., Sahasrabuddhe A.A., Kumar A., Mitra K., Siddiqi M.I., Gupta C.M. An unconventional form of actin in protozoan hemoflagellate, Leishmania. J. Biol. Chem. 2008, 283:22760-22773.
12. Keller, R. Optimizing the Process of Nuclear Magnetic Resonance Spectrum Analysis and Computer Aided Resonance Assignment. Diss. ETH no. 15947, Swiss Federal Institute of Technology, Zurich, 2005.
13. Koradi R., Billeter M., Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 1996, 14:51-55.
14. Lappalainen P., Fedorov E.V., Fedorov A.A., Almo S.C., Drubin D.G. Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis. EMBO J. 1997, 16:5520-5530.
15. Linge J.P., Williams M.A., Spronk A.E.M., Bonvin A.M., Nilges M. Refinement of protein structures in explicit solvent. Proteins 2003, 50:496-506.
16. Lipari G., Szabo A. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 1982, 104:4546-4559.
17. Lipari G., Szabo A. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Theory and range of validity. J. Am. Chem. Soc. 1982, 104:4559-4570.
18. Mandel A.M., Akke M., Palmer A.G. Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme. J. Mol. Biol. 1995, 246:144-163.
19. Mehta S., Sibley L.D. Toxoplasma gondii actin depolymerizing factor acts primarily to sequester G-actin. J. Biol. Chem. 2009, 285:6835-6847.
20. Moriyama K., Yahara I. The actin-severing activity of cofilin is exerted by the interplay of three distinct sites on cofilin and essential for cell viability. Biochem. J. 2002, 365:147-155.
21. Moriyama K., Yonezawa N., Sakai H., Yahara I., Nishida E. Mutational analysis of an actin-binding site of cofilin and characterization of chimeric proteins between cofilin and destrin. J. Biol. Chem. 1992, 267:7240-7244.
22. Ono S. Regulation of actin filament dynamics by actin depolymerizing factor/cofilin and actin-interacting protein 1: new blades for twisted filaments. Biochemistry 2003, 42:13363-13370.
23. Ono S., Baillie D.L., Benian G.M. J. Cell Biol. 1999, 145:491-502.
24. Ono S., Baillie D.L., Benian G.M. UNC-60B, an ADF/cofilin family protein, is required for proper assembly of actin into myofibrils in Caenorhabditis elegans body wall muscle. J. Cell. Biol. 1999, 145:491-502.
25. Ono S., McGough A., Pope B.J., Tolbert V.T., Bui A., Pohl J., Benian G.M., Gernert K.M., Weeds A.G. J. Biol. Chem. 2001, 276:5952-5958.
26. Paavilainen V.O., Oksanen E., Goldman A., Lappalainen P. Structure of the actin-depolymerizing factor homology domain in complex with actin. J. Cell. Biol. 2008, 182:51-59.
27. Palmer A.G., Rance M., Wright P.E. Intramolecular motions of a zinc finger DNA binding domain from Xfin characterized by proton detected natural abundance C-12 heteronuclear NMR-spectroscopy. J. Am. Chem. Soc. 1991, 113:4371-4380.
28. Pardee J.D., Spudich J.A. Methods Enzymol. 1982, 85:164-181.
29. Pathak P.P., Pulavarti S.V.S.R.K., Jain A., Sahasrabuddhe A.A., Gupta C.M., Arora A. NMR assignment of actin depolymerizing and dynamics regulatory protein from Leishmania donovani. Biomol. NMR Assignments 2009, 3:265-267.
30. Pope B.J., Gonsior S.M., Yeoh S., McGough A., Weeds A.G. Uncoupling actin filament fragmentation by cofilin from increased subunit turnover. J. Mol. Biol. 2000, 298:649-661.
31. Pope B.J., Zierler-Gould K.M., Kuhne R., Weeds A.G., Ball L.J. Solution structure of human cofilin: actin binding, pH sensitivity, and relationship to actin depolymerizing factor. J. Biol. Chem. 2004, 279:4840-4848.
32. Pulavarti S.V.S.R.K., Jain A., Pathak P.P., Mahmood A., Arora A. Solution structure and dynamics of peptidyl-tRNA hydrolase from Mycobacterium tuberculosis H37Rv. J. Mol. Biol. 2008, 378:165-177.
33. Roger C., Loria J.P. FAST-Modelfree: a program for rapid automated analysis of solution NMR spin relaxation data. J. Biomol. NMR 2003, 26:203-213.
34. Sahasrabuddhe A.A., Bajpai V.K., Gupta C.M. A novel form of actin in Leishmania: molecular characterization, subcellular localization and association with subpellicular microtubules. Mol. Biochem. Parasitol. 2004, 134:105-114.
35. Shen Y., Delaglio F., Cornilescu G., Bax A. TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J. Biomol. NMR 2009, 44:213-223.
36. Tammana T.V.S., Sahasrabuddhe A.A., Mitra K., Bajpai V.K., Gupta C.M. Actin-depolymerizing factor, ADF/cofilin, is essentially required in assembly of Leishmania flagellum. Mol. Microbiol. 2008, 70:837-852.
37. Vriend G. WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 1990, 8:52-56.
38. Yeoh S., Pope B., Mannherz H.G., Weeds A. Determining the differences in actin binding by human ADF and cofilin. J. Mol. Biol. 2002, 315:911-925.
39. Yonezawa N., Nishida E., Sakai H. PH control of actin polymerization by cofilin. J. Biol. Chem. 1985, 260:14410-14412.