Structural plasticity of functional actin: Pictures of actin binding protein and polymer interfaces

Structure

Volumn 11, Issue 10, 2003, Pages 1279-1289

  Rommelaere, Heidi ^a   Waterschoot, Davy ^a   Neirynck, Katrien ^a   Vandekerckhove, Joël ^a   Ampe, Christophe ^a  

^a DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; ALANINE; ALPHA ACTIN; BETA ACTIN; POLYMER;

ARTICLE; CELL SHAPE; CYTOSKELETON; MODEL; MUTAGENESIS; PLASTICITY; POLYMERIZATION; PRIORITY JOURNAL;

EID: 0141706541     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2003.09.002     Document Type: Article

References (34)

1. An H.S., Mogami K. Isolation of 88F actin mutants of Drosophila melanogaster and possible alterations in the mutant actin structures. J. Mol. Biol. 260:1996;492-505.
2. Ballweber E., Hannappel E., Huff T., Stephan H., Haener M., Taschner N., Stoffler D., Aebi U., Mannherz H.G. Polymerisation of chemically cross-linked actin:thymosin beta(4) complex to filamentous actin. alteration in helical parameters and visualisation of thymosin beta(4) binding on F-actin J. Mol. Biol. 315:2002;613-625.
3. Crosbie R.H., Miller C., Cheung P., Goodnight T., Muhlrad A., Reisler E. Structural connectivity in actin. effect of C-terminal modifications on the properties of actin Biophys. J. 67:1994;1957-1964.
4. De La Cruz E.M., Ostap E.M., Brundage R.A., Reddy K.S., Sweeney H.L., Safer D. Thymosin-beta(4) changes the conformation and dynamics of actin monomers. Biophys. J. 78:2000;2516-2527.
5. Gao Y., Thomas J.O., Chow R.L., Lee G.H., Cowan N.J. A cytoplasmic chaperonin that catalyzes beta-actin folding. Cell. 69:1992;1043-1050.
6. Hennessey E.S., Drummond D.R., Sparrow J.C. Molecular genetics of actin function. Biochem. J. 291:1993;657-671.
7. Holmes K.C., Popp D., Gebhard W., Kabsch W. Atomic model of the actin filament. Nature. 347:1990;44-49.
8. Holtzman D.A., Wertman K.F., Drubin D.G. Mapping actin surfaces required for functional interactions in vivo. J. Cell Biol. 126:1994;423-432.
9. Ilkovski B., Cooper S.T., Nowak K., Ryan M.M., Yang N., Schnell C., Durling H.J., Roddick L.G., Wilkinson I., Kornberg A.J.et al. Nemaline myopathy caused by mutations in the muscle alpha-skeletal- actin gene. Am. J. Hum. Genet. 68:2001;1333-1343.
10. Kabsch W., Mannherz H.G., Suck D., Pai E.F., Holmes K.C. Atomic structure of the actin:DNase I complex. Nature. 347:1990;37-44.
11. Lin C.S., Ng S.Y., Gunning P., Kedes L., Leavitt J. Identification and order of sequential mutations in beta-actin genes isolated from increasingly tumorigenic human fibroblast strains. Proc. Natl. Acad. Sci. USA. 82:1985;6995-6999.
12. Lorenz M., Popp D., Holmes K.C. Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234:1993;826-836.
13. McCormack E.A., Rohman M.J., Willison K.R. Mutational screen identifies critical amino acid residues of beta-actin mediating interaction between its folding intermediates and eukaryotic cytosolic chaperonin CCT. J. Struct. Biol. 135:2001;185-197.
14. McLaughlin P.J., Gooch J.T., Mannherz H.G., Weeds A.G. Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature. 364:1993;685-692.
15. Mendelson R.A., Morris E. The structure of F-actin. Results of global searches using data from electron microscopy and X-ray crystallography. J. Mol. Biol. 240:1994;138-154.
16. Mounier N., Sparrow J.C. Structural comparisons of muscle and nonmuscle actins give insights into the evolution of their functional differences. J. Mol. Evol. 44:1997;89-97.
17. Nowak K.J., Wattanasirichaigoon D., Goebel H.H., Wilce M., Pelin K., Donner K., Jacob R.L., Hubner C., Oexle K., Anderson J.R.et al. Mutations in the skeletal muscle alpha-actin gene in patients with actin myopathy and nemaline myopathy. Nat. Genet. 23:1999;208-212.
18. Nunoi H., Yamazaki T., Tsuchiya H., Kato S., Malech H.L., Matsuda I., Kanegasaki S. A heterozygous mutation of beta-actin associated with neutrophil dysfunction and recurrent infection. Proc. Natl. Acad. Sci. USA. 96:1999;8693-8698.
19. Olson T.M., Michels V.V., Thibodeau S.N., Tai Y.S., Keating M.T. Actin mutations in dilated cardiomyopathy, a heritable form of heart failure. Science. 280:1998;750-752.
20. Otterbein L.R., Cosio C., Graceffa P., Dominguez R. Crystal structures of the vitamin D-binding protein and its complex with actin. structural basis of the actin-scavenger system Proc. Natl. Acad. Sci. USA. 99:2002;8003-8008.
21. Pardee J.D., Spudich J.A. Purification of muscle actin. Methods Cell Biol. 24:1982;271-289.
22. Razzaq A., Schmitz S., Veigel C., Molloy J.E., Geeves M.A., Sparrow J.C. Actin residue glu(93) is identified as an amino acid affecting myosin binding. J. Biol. Chem. 274:1999;28321-28328.
23. Reichert A., Heintz D., Echner H., Voelter W., Faulstich H. Identification of contact sites in the actin-thymosin beta 4 complex by distance-dependent thiol cross-linking. J. Biol. Chem. 271:1996;1301-1308.
24. Robbens J., Louahed J., De Pestel K., Van Colen I., Ampe C., Vandekerckhove J., Renauld J.C. Murine adseverin (D5), a novel member of the gelsolin family, and murine adseverin are induced by interleukin-9 in T-helper lymphocytes. Mol. Cell Biol. 18:1998;4589-4596.
25. Robinson R.C., Mejillano M., Le V.P., Burtnick L.D., Yin H.L., Choe S. Domain movement in gelsolin. a calcium-activated switch Science. 286:1999;1939-1942.
26. Rommelaere H., Van Troys M., Gao Y., Melki R., Cowan N.J., Vandekerckhove J., Ampe C. Eukaryotic cytosolic chaperonin contains t-complex polypeptide 1 and seven related subunits. Proc. Natl. Acad. Sci. USA. 90:1993;11975-11979.
27. Rommelaere H., De Neve M., Melki R., Vandekerckhove J., Ampe C. The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins. Biochemistry. 38:1999;3246-3257.
28. Safer D. An electrophoretic procedure for detecting proteins that bind actin monomers. Anal. Biochem. 178:1989;32-37.
29. Safer D., Sosnick T.R., Elzinga M. Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends. Biochemistry. 36:1997;5806-5816.
30. Schagger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:1987;368-379.
31. Schutt C.E., Myslik J.C., Rozycki M.D., Goonesekere N.C., Lindberg U. The structure of crystalline profilin-beta-actin. Nature. 365:1993;810-816.
32. Steinmetz M.O., Stoffler D., Muller S.A., Jahn W., Wolpensinger B., Goldie K.N., Engel A., Faulstich H., Aebi U. Evaluating atomic models of F-actin with an undecagold-tagged phalloidin derivative. J. Mol. Biol. 276:1998;1-6.
33. Vainberg I.E., Lewis S.A., Rommelaere H., Ampe C., Vandekerckhove J., Klein H.L., Cowan N.J. Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin. Cell. 93:1998;863-873.
34. Wertman K.F., Drubin D.G., Botstein D. Systematic mutational analysis of the yeast ACT1 gene. Genetics. 132:1992;337-350.