This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Weber, M. H. W.
Right arrow Articles by Graumann, P. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Weber, M. H. W.
Right arrow Articles by Graumann, P. L.

 Previous Article  |  Next Article 

Journal of Bacteriology, November 2001, p. 6435-6443, Vol. 183, No. 21
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.21.6435-6443.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Localization of Cold Shock Proteins to Cytosolic Spaces Surrounding Nucleoids in Bacillus subtilis Depends on Active Transcription

Michael H. W. Weber, Arsen V. Volkov, Ingo Fricke, Mohamed A. Marahiel, and Peter L. Graumann*

Biochemie, Fachbereich Chemie, Philipps-Universität Marburg, 35032 Marburg, Germany

Received 18 June 2001/Accepted 21 June 2001

Using immunofluorescence microscopy and a fusion of a cold shock protein (CSP), CspB, to green fluorescent protein (GFP), we showed that in growing cells Bacillus subtilis CSPs specifically localize to cytosolic regions surrounding the nucleoid. The subcellular localization of CSPs is influenced by the structure of the nucleoid. Decondensed chromosomes in smc mutant cells reduced the sizes of the regions in which CSPs localized, while cold shock-induced chromosome compaction was accompanied by an expansion of the space in which CSPs were present. As a control, histone-like protein HBsu localized to the nucleoids, while beta -galactosidase and GFP were detectable throughout the cell. After inhibition of translation, CspB-GFP was still present around the nucleoids in a manner similar to that in cold-shocked cells. However, in stationary-phase cells and after inhibition of transcription, CspB was distributed throughout the cell, indicating that specific localization of CspB depends on active transcription and is not due to simple exclusion from the nucleoid. Furthermore, we observed that nucleoids are more condensed and frequently abnormal in cspB cspC and cspB cspD double-mutant cells. This suggests that the function of CSPs affects chromosome structure, probably through coupling of transcription to translation, which is thought to decondense nucleoids. In addition, we found that cspB cspD and cspB cspC double mutants are defective in sporulation, with a block at or before stage 0. Interestingly, CspB and CspC are depleted from the forespore compartment but not from the mother cell. In toto, our findings suggest that CSPs localize to zones of newly synthesized RNA, coupling transcription with initiation of translation.

* Corresponding author. Mailing address: Biochemie, Fachbereich Chemie, Hans-Meerwein-Straße, Philipps-Universität Marburg, 35032 Marburg, Germany. Phone: 49 (0) 6421 2825539. Fax: 49 (0) 6421 2822191. E-mail: graumann{at}chemie.uni-marburg.de.

Journal of Bacteriology, November 2001, p. 6435-6443, Vol. 183, No. 21
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.21.6435-6443.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Simmons, L. A., Grossman, A. D., Walker, G. C. (2008). Clp and Lon Proteases Occupy Distinct Subcellular Positions in Bacillus subtilis. J. Bacteriol. 190: 6758-6768 [Abstract] [Full Text]  
  • Castiglioni, P., Warner, D., Bensen, R. J., Anstrom, D. C., Harrison, J., Stoecker, M., Abad, M., Kumar, G., Salvador, S., D'Ordine, R., Navarro, S., Back, S., Fernandes, M., Targolli, J., Dasgupta, S., Bonin, C., Luethy, M. H., Heard, J. E. (2008). Bacterial RNA Chaperones Confer Abiotic Stress Tolerance in Plants and Improved Grain Yield in Maize under Water-Limited Conditions. Plant Physiol. 147: 446-455 [Full Text]  
  • Budde, I., Steil, L., Scharf, C., Volker, U., Bremer, E. (2006). Adaptation of Bacillus subtilis to growth at low temperature: a combined transcriptomic and proteomic appraisal.. Microbiology 152: 831-853 [Abstract] [Full Text]  
  • Hunger, K., Beckering, C. L., Wiegeshoff, F., Graumann, P. L., Marahiel, M. A. (2006). Cold-Induced Putative DEAD Box RNA Helicases CshA and CshB Are Essential for Cold Adaptation and Interact with Cold Shock Protein B in Bacillus subtilis. J. Bacteriol. 188: 240-248 [Abstract] [Full Text]  
  • Beckering, C. L., Steil, L., Weber, M. H. W., Volker, U., Marahiel, M. A. (2002). Genomewide Transcriptional Analysis of the Cold Shock Response in Bacillus subtilis. J. Bacteriol. 184: 6395-6402 [Abstract] [Full Text]  
  • Kaan, T., Homuth, G., Mader, U., Bandow, J., Schweder, T. (2002). Genome-wide transcriptional profiling of the Bacillus subtilis cold-shock response. Microbiology 148: 3441-3455 [Abstract] [Full Text]  
  • Weber, M. H. W., Fricke, I., Doll, N., Marahiel, M. A. (2002). CSDBase: an interactive database for cold shock domain-containing proteins and the bacterial cold shock response. Nucleic Acids Res 30: 375-378 [Abstract] [Full Text]  
  • Weber, M. H. W., Beckering, C. L., Marahiel, M. A. (2001). Complementation of Cold Shock Proteins by Translation Initiation Factor IF1 In Vivo. J. Bacteriol. 183: 7381-7386 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»