Structure and dynamics of the actin filament

Biochemistry

Volumn 44, Issue 9, 2005, Pages 3166-3175

  Guan, Jing Qu ^a   Takamoto, Keiji ^a   Almo, Steven C ^a   Reisler, Emil ^b   Chance, Mark R ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; MASS SPECTROMETRY; MATHEMATICAL MODELS; MOLECULAR STRUCTURE; MONOMERS; X RAY ANALYSIS;

ACTIN; HYDROXYL RADICALS; PROTEOLYSIS; SYNCHROTRON X-RAY RADIOLYSIS;

ADENOSINETRIPHOSPHATE;

F ACTIN; G ACTIN; HYDROXYL RADICAL; NUCLEOTIDE; PEPTIDE; POLYPHOSPHATE; POTASSIUM CHLORIDE;

ACTIN FILAMENT; ARTICLE; CRYSTAL STRUCTURE; DEUTERIUM HYDROGEN EXCHANGE; DYNAMICS; ELECTRON MICROSCOPY; LIGHT SCATTERING; MASS SPECTROMETRY; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PURIFICATION; RADIOLYSIS; STRUCTURE ANALYSIS; SYNCHROTRON;

ACTINS; ADENOSINE TRIPHOSPHATE; ANIMALS; LIGHT; MAGNESIUM; MASS SPECTROMETRY; MICROFILAMENTS; MODELS, MOLECULAR; OXIDATION-REDUCTION; POLYMERS; POTASSIUM CHLORIDE; PROTEIN FOOTPRINTING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RABBITS; SCATTERING, RADIATION; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS;

EID: 14644435764     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048021j     Document Type: Article

References (40)

1. Pollard, T. D., Blanchoin, L., and Mullins, R. D. (2001) Actin dynamics, J. Cell Sci. 114, 3-4.
2. Pollard, T. D., Blanchoin, L., and Mullins, R. D. (2000) Molecular mechanisms controlling actin filament dynamics in nonmuscle cells, Annu. Rev. Biophys. Biomol. Struct. 29, 545-576.
3. Chen, H., Bernstein, B. W., and Bamburg, J. R. (2000) Regulating actin-filament dynamics in vivo, Trends Biochem. Sci. 25, 19-23.
4. Otterbein, L. R., Graceffa, P., and Dominguez, R. (2001) The crystal structure of uncomplexed actin in the ADP state, Science 295, 708-711.
5. Graceffa, P., and Dominguez, R. (2003) Crystal structure of monomeric actin in the ATP state. Structural basis of nucleotide-dependent actin dynamics, J. Biol. Chem. 278, 34172-34180.
6. Kabsch, W., Mannherz, H. G., Suck, D., Pai, E. F., and Holmes, K. C. (1990) Atomic structure of the actin:DNase I complex, Nature 347, 37-44.
7. Kabsch, W., and Holmes, K. C. (1995) The actin fold, FASEB J. 9, 167-174.
8. Schutt, C. E., Myslik, J. C., Rozycki, M. D., Goonesekere, N. C. W., and Lindberg, U. (1993) The structure of crystalline profilin: β-Actin. Nature 365, 810-816.
9. McLaughlin, P. J., Gooch, J. T., Mannherz, H. G., and Weeds, A, G, (1993) Structure of gelsolin segment 1-actin complex and the mechanism of filament severing, Nature 364, 685-692.
10. Otterbein, L. R., Cosio, C., Graceffa, P., and Dominguez, R. (2002) Crystal structures of the vitamin D-binding protein and its complex with actin: structural basis of the actin-scavenger system, Proc. Natl. Acad. Sci. U.S.A. 99, 8003-8008.
11. Vorobiev, S., Strokopytov, B., Drubin, D. G., Frieden, C., Ono, S., Condeelis, J., Rubenstein, P. A., and Almo, S. C. (2003) The structure of nonvertebrate actin: Implications for the ATP hydrolytic mechanism, Proc. Natl. Acad. Sci. U.S.A. 100, 5760-5765.
12. Holmes, K. C., Popp, D., Gebhard, W., and Kabsch, W. (1990) Atomic model of the actin filament, Nature 347, 44-49.
13. Lorenz, M., Popp, D., and Holmes, K. C. (1993) Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm, J. Mol. Biol. 234, 826-836.
14. Pollard, T. D., and Cooper, J. A. (1986) Actin and actin-binding proteins. A critical evaluation of mechanisms and functions, Annu. Rev. Biochem. 55, 987-1035.
15. Guan, J. Q., Almo, S., and Chance, M. R. (2004) Synchrotron radiolysis and mass spectrometry: A new approach to research on the actin cytoskeleton, Acc. Chem. Res. 37, 221-229.
16. Guan, J. Q., Almo, S. C., Reisler, E., and Chance, M. R. (2003) Structural reorganization of proteins revealed by radiolysis and mass spectrometry: G-actin solution structure is divalent cation dependent, Biochemistry 42, 11992-12000.
17. Kiselar, J. G., Maleknia, S. D., Sullivan, M., Downard, K. M., and Chance, M. R. (2002) Hydroxyl radical probe of protein surfaces using synchrotron X-ray radiolysis and mass spectrometry, Int. J. Radiat. Biol. 78, 101-114.
18. Kiselar, J. G., Janmey, P. A., Almo, S. C., and Chance, M. R. (2003) Structural analysis of gelsolin using synchrotron protein footprinting, Mol. Cell. Proteomics 2, 1120-1132.
19. 2+-dependent activation of gelsolin by using synchrotron footprinting, Proc. Natl. Acad. Sci. U.S.A. 100, 3942-3947.
20. Liu, R., Guan, J. Q., Zak, O., Aisen, P., and Chance, M. R. (2003) Structural reorganization of transferrin C-lobe and transferrin receptor upon complex formation: C-lobe to the receptor helical domain, Biochemistry 42, 12447-12454.
21. Guan, J. Q., Vorobiev, S., Almo, S. C., and Chance, M. R. (2002) Mapping the G-actin binding surface of cofilin using synchrotron protein footprinting, Biochemistry 41, 5765-5775.
22. Zhang, Z., and Smith, D. L. (1993) Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation, Protein Sci. 2, 522-531.
23. Katta, V. and Chait, B. T. (1993) Hydrogen/deuterium exchange electrospray ionization mass spectrometry: A method for probing protein conformational changes in solution. J. Am. Chem. Soc. 115, 6317-6321.
24. Englander, S. W., and Kallenbach, N. R. (1983) Hydrogen exchange and structural dynamics of proteins and nucleic acids, Q. Rev. Biophys. 16, 521-655.
25. Chik, J. K., and Schriemer, D. C. (2003) Hydrogen/deuterium exchange mass spectrometry of actin in various biochemical contexts, J. Mol. Biol. 334, 373-385.
26. Spudich, J. A., and 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.
27. Sclavi, B., Woodson, S., Sullivan, M., Chance, M. R., and Brenowitz, M. (1997) Time-resolved synchrotron X-ray "footprinting", a new approach to the study of nucleic acid structure and function: Application to protein - DNA interactions and RNA folding, J. Mol. Biol. 266, 144-159.
28. Ralston, C. Y., Sclavi, B., Sullivan, M., Deras, M. L., Woodson, S. A., Chance, M. R., and Brenowitz, M. (2000) Time-resolved synchrotron X-ray footprinting and its application to RNA folding, Methods Enzymol. 317, 353-368.
29. Maleknia, S. D., Ralston, C. Y., Brenowitz, M. D., Downard, K. M., and Chance, M. R. (2001) Determination of macromolecular folding and structure by synchrotron X-ray radiolysis techniques, Anal. Biochem. 289, 103-115.
30. Gupta, S., Mangel, W. F., McGrath, W. J., Perek J. L., Lee, D. W., Takamoto, K., and Chance, M. R. (2004) DNA binding provides a molecular strap activating the adenovirus proteinase, Mol. Cell. Proteomics 3, 950-959.
31. Ralston, C. Y., He, Q., Brenowitz, M., and Chance, M. R. (2000) Stability and cooperativity of individual tertiary contacts in RNA revealed through chemical denaturation, Nat. Struct. Biol. 7, 371-374.
32. Uchida, T., Takamoto, K., He, Q., Chance, M. R., and Brenowitz, M. (2003) Multiple monovalent ion-dependent patways for the folding of the L-21 Tetrahymena thermophila ribozyme, J. Mol. Biol. 328, 463-478.
33. Egelman, E. H., and Orlova, A. (1995) New insights into actin filament dynamics, Curr. Opin. Struct. Biol. 5, 172-180.
34. Orlova, A., and Egelman, E. H. (1995) Structural dynamics of F-actin: I. Changes in the C terminus, J. Mol. Biol. 245, 582-597.
35. Oda, T., Makino, K., Yamashita, I., Namba, K., and Maeda, Y. (1998) Effect of the length and effective diameter of F-actin on the filament orientation in liquid crystalline sols measured by X-ray fiber diffraction, Biophys. J. 75, 2672-2681.
36. Oda, T., Makino, K., Yamashita, I., Namba, K., and Maeda, Y. (2001) Distinct structural changes detected by X-ray fiber diffraction in stabilization of F-actin by lowing pH and increasing ionic strength, Biophys. J. 80, 841-851.
37. 1H nuclear magnetic resonance spectroscopy, FEBS Lett. 351, 405-410.
38. Kuang, B., and Rubenstein, P. A. (1997) Beryllium fluoride and phalloidin restore polymerizability of a mutant yeast actin (V266G, L267G) with severely decreased hydrophobicity in a subdomain 3/4 loop, J. Biol. Chem. 272, 1237-1247.
39. Shvetsov, A., Musib, R., Phillips, M., Rubenstein, P. A., and Reisler, E. (2002) Locking the hydrophobic loop 262-274 to G-actin surface by a disulfide bridge prevents filament formation, Biochemistry 41, 10787-10793.
40. Kim, E., Wriggers, W., Phillips, M., Kobabi, K., Rubenstein, P. A., and Reisler, E. (2000) Cross-linking constraints on F-actin structure, J. Mol. Biol. 299, 421-429.