Polar positional information in Escherichia coli spherical cells

Biochemical and Biophysical Research Communications

Volumn 353, Issue 2, 2007, Pages 493-500

  Pradel, Nathalie ^a   Santini, Claire Lise ^a   Bernadac, Alain ^a   Shih, Yu Ling ^b   Goldberg, Marcia B ^c   Wu, Long Fei ^a  

^a CNRS   (France)

^b UNIVERSITY OF CONNECTICUT HEALTH CENTER   (United States)

^c MASSACHUSETTS GENERAL HOSPITAL   (United States)

Author keywords

GFP; mCherry; MreB; Periplasm; Polar localization information; Spherical cells

Indexed keywords

MARKER; TRANSACTIVATOR PROTEIN;

ANIMAL CELL; ARTICLE; BACTERIAL CELL; BACTERIAL KINETICS; CONTROLLED STUDY; CYTOPLASM; ESCHERICHIA COLI; FLUORESCENCE; INTERCELLULAR SPACE; NONHUMAN; POLARIZATION; PRIORITY JOURNAL; PROTEIN LOCALIZATION; SPONTANEOUS MUTATION;

BACTERIAL PROTEINS; CELL POLARITY; DNA-BINDING PROTEINS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MEMBRANE PROTEINS; TRANSCRIPTION FACTORS;

ESCHERICHIA COLI; SHIGELLA;

EID: 33845874640     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.12.054     Document Type: Article

References (36)

1. Janakiraman A., and Goldberg M.B. Recent advances on the development of bacterial poles. Trends Microbiol. 12 (2004) 518-525
2. Goldberg M.B., Barzu O., Parsot C., and Sansonetti P.J. Unipolar localization and ATPase activity of IcsA, a Shigella flexneri protein involved in intracellular movement. J. Bacteriol. 175 (1993) 2189-2196
3. Brandon L.D., Goehring N., Janakiraman A., Yan A.W., Wu T., Beckwith J., and Goldberg M.B. IcsA, a polarly localized autotransporter with an atypical signal peptide, uses the Sec apparatus for secretion, although the Sec apparatus is circumferentially distributed. Mol. Microbiol. 50 (2003) 45-60
4. Charles M., Perez M., Kobil J.H., and Goldberg M.B. Polar targeting of Shigella virulence factor IcsA in Enterobacteriacae and Vibrio. Proc. Natl. Acad. Sci. USA 98 (2001) 9871-9876
5. Cabeen M.T., and Jacobs-Wagner C. Bacterial cell shape. Nat. Rev. Microbiol. 3 (2005) 601-610
6. Shih Y.L., Kawagishi I., and Rothfield L. The MreB and Min cytoskeletal-like systems play independent roles in prokaryotic polar differentiation. Mol. Microbiol. 58 (2005) 917-928
7. Nilsen T., Yan A.W., Gale G., and Goldberg M.B. Presence of multiple sites containing polar material in spherical Escherichia coli cells that lack MreB. J. Bacteriol. 187 (2005) 6187-6196
8. Janakiraman A., and Goldberg M.B. Evidence for polar positional information independent of cell division and nucleoid occlusion. Proc. Natl. Acad. Sci. USA 101 (2004) 835-840
9. Huitema E., Pritchard S., Matteson D., Radhakrishnan S.K., and Viollier P.H. Bacterial birth scar proteins mark future flagellum assembly site. Cell 124 (2006) 1025-1037
10. Lam H., Schofield W.B., and Jacobs-Wagner C. A landmark protein essential for establishing and perpetuating the polarity of a bacterial cell. Cell 124 (2006) 1011-1023
11. Scheffel A., Gruska M., Faivre D., Linaroudis A., Plitzko J.M., and Schuler D. An acidic protein aligns magnetosomes along a filamentous structure in magnetotactic bacteria. Nature 440 (2006) 110-114
12. Komeili A., Li Z., Newman D.K., and Jensen G.J. Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK. Science 311 (2006) 242-245
13. Pradel N., Santini C.-L., Bernadac A., Fukumori Y., and Wu L.-F. Biogenesis of actin-like bacterial cytoskeletal filaments destined for positioning prokaryotic magnetic organelles. Proc. Natl. Acad. Sci. USA 103 (2006) 17485-17489
14. Figge R.M., Divakaruni A.V., and Gober J.W. MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus. Mol. Microbiol. 51 (2004) 1321-1332
15. Divakaruni A.V., Loo R.R., Xie Y., Loo J.A., and Gober J.W. The cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in Caulobacter crescentus. Proc. Natl. Acad. Sci. USA 102 (2005) 18602-18607
16. Dye N.A., Pincus Z., Theriot J.A., Shapiro L., and Gitai Z. Two independent spiral structures control cell shape in Caulobacter. Proc. Natl. Acad. Sci. USA 102 (2005) 18608-18613
17. Santini C.-L., Bernadac A., Zhang M., Chanal A., Ize B., Blanco C., and Wu L.-F. Translocation of jellyfish green fluorescent protein via the Tat system of Escherichia coli and change of its periplasmic localization in response to osmotic up-shock. J. Biol. Chem. 276 (2001) 8159-8164
18. Miesenbock G., De Angelis D.A., and Rothman J.E. Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins. Nature 394 (1998) 192-195
19. Miller J.H. Experiments in Molecular Genetics (1972), Cold Spring Harbor Laboratory, Cold Spring Harbor, New York
20. Anba J., Bernadac A., Pages J.-M., and Lazdunski C. The periseptal annulus in Escherichia coli. Biol. Cell 50 (1984) 273-278
21. Wachi M., Doi M., Okada Y., and Matsuhashi M. New mre genes mreC and mreD, responsible for formation of the rod shape of Escherichia coli cells. J. Bacteriol. 171 (1989) 6511-6516
22. Wachi M., Doi M., Tamaki S., Park W., Nakajima-Iijima S., and Matsuhashi M. Mutant isolation and molecular cloning of mre genes, which determine cell shape, sensitivity to mecillinam, and amount of penicillin-binding proteins in Escherichia coli. J. Bacteriol. 169 (1987) 4935-4940
23. Daniel R.A., and Errington J. Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell. Cell 113 (2003) 767-776
24. Ishino F., Park W., Tomioka S., Tamaki S., Takase I., Kunugita K., Matsuzawa H., Asoh S., Ohta T., Spratt B.G., et al. Peptidoglycan synthetic activities in membranes of Escherichia coli caused by overproduction of penicillin-binding protein 2 and rodA protein. J. Biol. Chem. 261 (1986) 7024-7031
25. Matsuzawa H., Hayakawa K., Sato T., and Imahori K. Characterization and genetic analysis of a mutant of Escherichia coli K-12 with rounded morphology. J. Bacteriol. 115 (1973) 436-442
26. Spratt B.G. Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proc. Natl. Acad. Sci. USA 72 (1975) 2999-3003
27. Kruse T., Bork-Jensen J., and Gerdes K. The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex. Mol. Microbiol. 55 (2005) 78-89
28. Gibbs K.A., Isaac D.D., Xu J., Hendrix R.W., Silhavy T.J., and Theriot J.A. Complex spatial distribution dynamics of an abundant Escherichia coli outer membrane protein LamB. Mol. Microbiol. 53 (2004) 1771-1783
29. Bayer M.E. Areas of adhesion between wall and membrane of Escherichia coli. J. Gen. Microbiol. 53 (1968) 395-404
30. Bayer M. The fusion sites between outer membrane and cytoplasmic membrane of bacteria: their role in membrane assembly and virus infection. In: Inouye M. (Ed). Bacterial Outer Membrane (1979), M. Wiley, New York 167-202
31. Woldringh C.L. Significance of plasmolysis spaces as markers for periseptal annuli and adhesion sites. Mol. Microbiol. 14 (1994) 597-607
32. Andersen C., Hughes C., and Koronakis V. Protein export and drug efflux through bacterial channel-tunnels. Curr. Opin. Cell Biol. 13 (2001) 412-416
33. Holland I.B., Schmitt L., and Young J. Type 1 protein secretion in bacteria, the ABC-transporter dependent pathway. Mol. Membr. Biol. 22 (2005) 29-39
34. Murakami S., and Yamaguchi A. Multidrug-exporting secondary transporters. Curr. Opin. Struct. Biol. 13 (2003) 443-452
35. Shiomi D., Banno S., Homma M., and Kawagishi I. Stabilization of polar localization of a chemoreceptor via its covalent modifications and its communication with a different chemoreceptor. J. Bacteriol. 187 (2005) 7647-7654
36. de Pedro M.A., Donachie W.D., Holtje J.V., and Schwarz H. Constitutive septal murein synthesis in Escherichia coli with impaired activity of the morphogenetic proteins RodA and penicillin-binding protein 2. J. Bacteriol. 183 (2001) 4115-4126