The axial α-helices and radial spokes in the core of the cryo-negatively stained complex flagellar filament of Pseudomonas rhodos: Recovering high-resolution details from a flexible helical assembly

Journal of Molecular Biology

Volumn 331, Issue 5, 2003, Pages 1093-1108

  Cohen Krausz, Sara ^a   Trachtenberg, Shlomo ^a  

^a HEBREW UNIVERSITY OF JERUSALEM   (Israel)

Author keywords

Bacterial flagella; Complex flagellar filaments; Correspondence analysis; Cryo electron microscopy; Flagellin

Indexed keywords

FLAGELLIN;

ALPHA HELIX; ARTICLE; CONTROLLED STUDY; DENSITY; ELECTRON MICROSCOPY; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PSEUDOMONAS; RHIZOBIUM; RHIZOBIUM LUPINI; SALMONELLA TYPHIMURIUM;

BACTERIA (MICROORGANISMS); METHYLOBACTERIUM RHODINUM; PSEUDOMONAS; PSEUDOMONAS RHODOS; RHIZOBIUM; RHIZOBIUM LUPINI; SALMONELLA TYPHIMURIUM;

EID: 0043166159     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00810-6     Document Type: Article

References (48)

1. Trachtenberg S., Hammel I. The rigidity of bacterial flagellar filaments and its relation to filament polymorphism. J. Struct. Biol. 109:1992;18-27.
2. Cohen-Krausz S., Trachtenberg S. Helical perturbations of the flagellar filament: Rhizobium lupini H13-3 at 13 Å resolution. J. Struct. Biol. 122:1998;267-282.
3. Cohen-Krausz S., Trachtenberg S. The structure of the helically perturbed flagellar filament of Pseudomonas rhodos: implications for the absence of the outer domain in other complex flagellins and for the flexibility of the radial spokes. Mol. Microbiol. 48:2003;1305-1316.
4. Trachtenberg S., DeRosier D.J., Aizawa S.-I., Macnab R.M. Pairwise perturbation of flagellin subunits. The structural basis for the differences between plain and complex bacterial flagellar filaments. J. Mol. Biol. 190:1986;569-576.
5. Trachtenberg S., DeRosier D.J., Macnab R.M. Three-dimensional structure of the complex flagellar filament of Rhizobium lupini and its relation to the structure of the plain filament. J. Mol. Biol. 195:1987;603-620.
6. Trachtenberg S., DeRosier D.J., Zemlin F., Beckman E. Non-helical perturbations of the flagellar filament: Salmonella typhimurium SJW117 at 9.6 Å resolution. J. Mol. Biol. 276:1998;759-773.
7. Trachtenberg S., Fishelov D., Ben-Artzi M. Bacterial flagellar microhydrodynamics: laminar flow over complex flagellar filaments, analog Archimedean screws and cylinders and its perturbations. Biophys. J. 85:2003;. in the press.
8. Scharf B. Real-time imaging of fluorescent flagellar filaments of Rhizobium lupini H13-3: flagellar rotation and pH induced polymorphic transitions. J. Bacteriol. 184:2002;5979-5986.
9. Götz R., Schmitt R. Rhizobium meliloti swims by unidirectional, intermittent rotation of right-handed flagellar helices. J. Bacteriol. 169:1987;3146-3150.
10. Sourjik V., Schmitt R. Different roles of CheY1 and CheY2 in the chemotaxis of Rhizobium meliloti. Mol. Microbiol. 22:1996;427-436.
11. Samatey F.A., Imada K., Nagashima S., Vonderviszt F., Yamamoto M., Namba K. Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling. Nature. 410:2001;331-337.
12. Mimori-Kiyosue Y., Vonderviszt F., Yamashita I., Fujiyoshi Y., Namba K. Direct interaction of flagellin termini essential for polymorphic ability of flagellar filament. Proc. Natl Acad. Sci. USA. 93:1996;15108-15113.
13. Mimori-Kiyosue Y., Vonderviszt F., Namba K. Locations of terminal segments of flagellin in the filament structure and their roles in polymerization and polymorphism. J. Mol. Biol. 270:1997;222-237.
14. Hyman H.C., Trachtenberg S. Point mutations that lock Salmonella typhimurium flagellar filaments in the straight right-handed and left-handed forms and their relation to filament superhelicity. J. Mol. Biol. 220:1991;79-88.
15. Trachtenberg S., DeRosier D.J. Three-dimensional reconstruction of the flagellar filament of Caulobacter cresentus. A flagellin lacking the outer domain and its amino acid sequence lacking an internal sequence. J. Mol. Biol. 202:1988;787-808.
16. Yoshioka K., Aizawa S.-I., Yamaguchi S. Flagellar filament structure and cell motility of Salmonella typhimurium mutants lacking part of the outer domain of flagellin. J. Bacteriol. 177:1995;1090-1093.
17. Kuwajima G. Construction of a minimum-size functional flagellin of Escherichia coli. J. Bacteriol. 170:1988;3305-3309.
18. Kuwajima G., Asaka J.-I., Fujiwara T., Fujiwara T., Nakano K., Kondo E. Presentation of an antigenic determinant from hen egg-white lysozyme on the flagellar filament of Escherichia coli. Biotechnology. 6:1988;1080-1083.
19. Mimori-Kiyosue Y., Yamashita I., Fujiyoshi Y., Yamaguchi S., Namba K. Role of outermost subdomain of Salmonella flagellin in the filament structure revealed by electron cryomicroscopy. J. Mol. Biol. 284:1998;521-530.
20. DeRosier D.J., Moore P.B. Reconstruction of three-dimensional images from electron micrographs of structures with helical symmetry. J. Mol. Biol. 52:1970;355-369.
21. Owen C., DeRosier D.J. A 13 Å map of the actin-scruin filament from the Limulus acrosomal process. J. Cell. Biol. 123:1993;337-344.
22. Owen C., Morgan D.G., DeRosier D.J. Image analysis of helical objects: the Brandeis helical package. J. Struct. Biol. 116:1996;167-175.
23. Scharf B., Schuster-Wolff-Buhring H., Rachel R., Schmitt R. Mutational analysis of the Rhizobium lupini H13-3 and Sinorhizobium meliloti flagellin genes: importance of flagellin A for flagellar filament structure and transcriptional regulation. J. Bacteriol. 183:2001;5334-5342.
24. Massover W.H. Is negative staining capable of high resolution? Microsc. Microanal. 7:2001;360-361.
25. Unwin P.N.T., Henderson R. Molecular structure determination by electron microscopy of unstained crystalline specimens. J. Mol. Biol. 94:1975;425-440.
26. Erickson H.P., Klug A. Measurement and compensation of defocusing and aberrations by Fourier processing of electron micrographs. Phil. Trans. Roy. Soc. London. 261:1971;105-118.
27. th International Congress on Electron microscopy. (Paris). vol. 1:1994;Les Editions de Physiques, Les Ulis, France.
28. Frank J. Three-dimensional Electron Microscopy of Macromolecular Assemblies. 1996;Academic Press, San Diego.
29. Bremer A., Henn C., Engel A., Baumeister W., Aebi U. Has negative staining still a place in biomacromolecular electron microscopy? Ultramicroscopy. 46:1992;85-111.
30. Massover W.H., Fun Lai P.F., Marsh P. Negative staining permits 4.0 Å resolution with low-dose electron diffraction of catalase crystals. Ultramicroscopy. 90:2001;7-12.
31. Glaeser R.M. Limitations to significant information in biological electron microscopy as a result of radiation damage. J. Ultrastruct. Res. 36:1971;466-482.
32. Adrian M., Dubochet J., Fuller S.D., Harris J.R. Cryo negative staining. Micron. 29:1998;145-160.
33. De Carlo S., El-Bez C., Alvarez-Rua C., Borge J., Dubochet J. Cryo-negative staining reduces electron-beam sensitivity of vitrified biological particles. J. Struct. Biol. 138:2002;216-226.
34. Mimori Y., Yamashita I., Murata K., Fujiyoshi Y., Yonekura K., Toyoshima C., Namba K. The structure of the R-type straight flagellar filament of Salmonella at 9 Å resolution by electron cryomicroscopy. J. Mol. Biol. 249:1995;69-87.
35. Morgan D.G., Owen C., Melanson L.A., DeRosier D.J. Structure of bacterial flagellar filaments at 11 Å resolution: packing of the α-helices. J. Mol. Biol. 249:1995;88-110.
36. Egelman E.H. A robust algorithm for the reconstruction of helical filaments using single-particle methods. Ultramicroscopy. 85:2000;225-234.
37. Frank J. Single particle imaging of macromolecules by cryo-electron microscopy. Annu. Rev. Biophys. Biomol. Struct. 31:2002;303-319.
38. Harauz G., Van Heel M. Exact filters for general geometry three-dimensional reconstruction. Optik. 73:1986;146-156.
39. Van Heel M., Gowen B., Matadeen R., Orlova E.V., Finn R., Pape T., et al. Single-particle electron cryo-microscopy: towards atomic resolution. Quart. Rev. Biophys. 33:2000;307-369.
40. Trachtenberg S. Fast-freezing devices for cryo-electron-microscopy. Micron. 24:1993;1-12.
41. Trachtenberg S. A fast-freezing device with a retractable environmental chamber, suitable for kinetic cryo-electron microscopy studies. J. Struct. Biol. 123:1998;45-55.
42. Salmon E.D., DeRosier D.J. A surveying optical diffractometer. J. Microsc. 123:1981;239-247.
43. Egelman E.H. An algorithm for straightening images of curved filamentous structures. Ultramicroscopy. 19:1986;367-374.
44. Stewart M., Kensler R.W., Levine R.J.C. Structure of Limulus telson muscle thick filaments. J. Mol. Biol. 153:1981;781-790.
45. Amos L.A. Combination of data from helical particles: correlation and selection. J. Mol. Biol. 99:1975;57-73.
46. Frank J., Radermacher M., Penczec P., Zhu J., Li Y., Ladjadj M., Leith A. SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116:1996;190-199.
47. Toyoshima C., Unwin N. Contrast transfer for frozen-hydrated specimens: determination from pairs of defocused images. Ultramicroscopy. 25:1988;279-292.
48. Trachtenberg S., DeRosier D.J. Three-dimensional structure of the frozen-hydrated flagellar filament. The left-handed filament of Salmonella typhimurium. J. Mol. Biol. 197:1987;581-601.