Evaluating atomic models of F-actin with an undecagold-tagged phalloidin derivative

Journal of Molecular Biology

Volumn 276, Issue 1, 1998, Pages 1-6

  Steinmetz, Michel O ^a   Stoffler, Daniel ^a   Müller, Shirley A ^a   Jahn, Werner ^c   Wolpensinger, Bettina ^a   Goldie, Kenneth N ^a,b   Engel, Andreas ^a   Faulstich, Heinz ^c   Aebi, Ueli ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

^b UNIVERSITY OF AUCKLAND   (New Zealand)

^c MAX PLANCK INSTITUTE FOR MEDICAL RESEARCH   (Germany)

Author keywords

3 D reconstructions; F actin; Image processing; Phalloidin; Scanning transmission electron microscopy

Indexed keywords

F ACTIN; PHALLOIDIN;

ACTIN FILAMENT; ARTICLE; BINDING SITE; BIOCHEMISTRY; CHEMICAL LABELING; MUSHROOM; NONHUMAN; PRIORITY JOURNAL; STOICHIOMETRY; TRANSMISSION ELECTRON MICROSCOPY;

BASIDIOMYCOTA;

EID: 0032512610     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1529     Document Type: Article

References (26)

1. Bartlett P.A., Bauer B., Singer S.J. Synthesis of water-soluble undecagold cluster compounds of potential importance in electron microscopic and otherstudies of biological systems. J. Am. Chem. Soc. 100:1978;5085-5089
2. Bremer A., Millonig R.C., Sütterlin R., Engel A., Pollard T.D., Aebi U. The structural basis for the intrinsic disorder of the F-actin filament the lateral slipping model. J. Cell Biol. 115:1991;689-703
3. Bremer A., Henn C., Goldie K.N., Engel A., Smith P.R., Aebi U. Towards atomic interpretation of F-actin filament three-dimensional reconstructions. J. Mol Biol. 742:1994;683-700
4. Engel A., Colliex C. Application of scanning transmission electron microscopy to the study of biological structure. Curr. Opin. Biotechnol. 4:1993;403-411
5. Faulstich H., Zobely S., Rinnerthaler G., Small J.V. Fluorescent phallotoxins as probes for filamentous actin. J. Muscle Res. Cell Motil. 9:1988;370-383
6. Holmes K.C., Popp D., Gebhard W., Kabsch W. Atomic model of the F-actin filament. Nature. 347:1990;44-49
7. Jahn W. Synthesis of water soluble undecagold clusters for specific labeling of proteins. Z. Naturforsch. 44b:1989;1313-1322
8. Kabsch W., Mannherz H.G., Suck D., Pai E., Holmes K.C. Atomic structure of the actin Nase I complex. Nature. 347:1990;37-44
9. 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
10. Lorenz M., Poole K.J.V., Popp D., Rosenbaum G., Holmes K.C. An atomic model of the unregulated thin filament obtained by X-ray fiber diffraction on oriented actin-tropomyosingels. J. Mol. Biol. 246:1995;108-119
11. McGough A., Way M., DeRosier D. Determination of the α-actinin binding site on actin filaments by cryoelectron microscopy and image analysis. J. Cell Biol. 126:1994;433-443
12. McGough A., Pope B., Chiu W., Weeds A.G. Cofilin changes the twist of F-actin Implications for actin filament dynamics and cellular function. J. Cell Biol. 138:1997;771-781
13. McLaughlin P.J., Gooch J.T., Mannherz H.G., Weeds A.G. The atomic structure of gelsolin segment 1 ctin complex and the mechanism of filament severing. Nature. 364:1993;685-692
14. Müller S.A., Goldie K.N., Bürki R., Häring R., Engel A. Factors influencing the precision of quantitative scanning transmission electron microscopy. Ultramicroscopy. 46:1992;317-334
15. Owen C., DeRosier D. A 13-Å map of the actin-scruin filament from the Limulus acrosomal process. J. Cell Biol. 123:1993;337-344
16. Rayment I., Holden H.M., Whittaker M., Yohn C.B., Lorenz M., Holmes K.C., Milligan R.A. Structure of the actin-myosin complex and its implication for muscle contraction. Science. 261:1993;58-65
17. Schmid M.F., Agris J.M., Jakana J., Matsudaira P., Chiu W. Three-dimensional structure of a single filament in the Limulus acrosomal bundle scruin binds to homologoushelix-loop-beta motifs in actin. J. Cell Biol. 124:1994;341-350
18. Schutt C.E., Lindberg U. Actin as the generator of tension during muscle contraction. Proc. Natl Acad. Sci. USA. 89:1992;319-323
19. Schutt C.E., Myslik J.C., Rozycki M.D., Goonesekere N.C.W., Lindberg U. The structure of crystalline profilin-β-actin. Nature. 365:1993;810-816
20. Schutt C.E., Rozycki M.D., Myslik J.C. A discourse on modeling F-actin. J. Struct. Biol. 115:1995;186-198
21. Schutt C.E., Rozycki M.D., Chik J., Lindberg U. Structural studies on the ribbon-to-helix transition in profilin ctin crystals. Biophys. J. 68:1995;12 s-18 s
22. Schutt C.E., Kreatsoulas C., Page R., Lindberg U. Plugging into actin's architectonic socket. Nature Struct. Biol. 4:1997;169-172
23. Steinmetz M.O., Goldie K.N., Aebi U. A correlative analysis of actin filament assembly, structure and dynamics. J. Cell Biol. 138:1997;559-574
24. Steinmetz M.O., Stoffler D., Hoenger A., Bremer A., Aebi U. Actin From cell biology to atomic detail. J. Struct. Biol. 119:1997;295-320
25. Vandekerckhove J., Deboben A., Nassal M., Wieland T. The phalloidin binding site of F-actin. EMBO J. 4:(11):1985;2815-2818
26. Wieland T., Hollosi M., Nassal M. δ-Aminophalloin, ein 7-Analoges des Phalloidins, und biochemisch nutzliche, auch fluoreszierendeDerivate. Liebig's Ann. Chem. 1983;1533-1540