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 Kanemori, M.
Right arrow Articles by Yura, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kanemori, M.
Right arrow Articles by Yura, T.

 Previous Article  |  Next Article 

Journal of Bacteriology, June 1999, p. 3674-3680, Vol. 181, No. 12
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

The ATP-Dependent HslVU/ClpQY Protease Participates in Turnover of Cell Division Inhibitor SulA in Escherichia coli

Masaaki Kanemori, Hideki Yanagi, and Takashi Yura*

HSP Research Institute, Kyoto Research Park, Kyoto 600-8813, Japan

Received 19 October 1998/Accepted 16 February 1999

Escherichia coli mutants lacking activities of all known cytosolic ATP-dependent proteases (Lon, ClpAP, ClpXP, and HslVU), due to double deletions [Delta hslVU and Delta (clpPX-lon)], cannot grow at low (30°C) or very high (45°C) temperatures, unlike those carrying either of the deletions. Such growth defects were particularly marked when the deletions were introduced into strain MG1655 or W3110. To examine the functions of HslVU and other proteases further, revertants that can grow at 30°C were isolated from the multiple-protease mutant and characterized. The revertants were found to carry a suppressor affecting either ftsZ (encoding a key cell division protein) or sulA (encoding the SulA inhibitor, which binds and inhibits FtsZ). Whereas the ftsZ mutations were identical to a mutation known to produce a protein refractory to SulA inhibition, the sulA mutations affected the promoter-operator region, reducing synthesis of SulA. These results suggested that the growth defect of the parental double-deletion mutant at a low temperature was due to the accumulation of excess SulA without DNA-damaging treatment. Consistent with these results, SulA in the double-deletion mutant was much more stable than that in the Delta (clpPX-lon) mutant, suggesting that SulA can be degraded by HslVU. As expected, purified HslVU protease degraded SulA (fused to the maltose-binding protein) efficiently in an ATP-dependent manner. These results suggest that HslVU as well as Lon participates in the in vivo turnover of SulA and that HslVU becomes essential for growth when the Lon (and Clp) protease level is reduced below a critical threshold.

* Corresponding author. Mailing address: HSP Research Institute, Kyoto Research Park, Kyoto 600-8813, Japan. Phone: (81)-75-315-8619. Fax: (81)-75-315-8659. E-mail: tyura{at}hsp.co.jp.

Journal of Bacteriology, June 1999, p. 3674-3680, Vol. 181, No. 12
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Koga, N., Kameda, T., Okazaki, K.-i., Takada, S. (2009). Paddling mechanism for the substrate translocation by AAA+ motor revealed by multiscale molecular simulations. Proc. Natl. Acad. Sci. USA 106: 18237-18242 [Abstract] [Full Text]  
  • Ruan, B., Palioura, S., Sabina, J., Marvin-Guy, L., Kochhar, S., LaRossa, R. A., Soll, D. (2008). Quality control despite mistranslation caused by an ambiguous genetic code. Proc. Natl. Acad. Sci. USA 105: 16502-16507 [Abstract] [Full Text]  
  • Mizrahi, I., Dagan, M., Biran, D., Ron, E. Z. (2007). Potential Use of Toxic Thermolabile Proteins To Study Protein Quality Control Systems. Appl. Environ. Microbiol. 73: 5951-5953 [Abstract] [Full Text]  
  • Kirkland, P. A., Reuter, C. J., Maupin-Furlow, J. A. (2007). Effect of proteasome inhibitor clasto-lactacystin-beta-lactone on the proteome of the haloarchaeon Haloferax volcanii. Microbiology 153: 2271-2280 [Abstract] [Full Text]  
  • Munavar, H., Zhou, Y., Gottesman, S. (2005). Analysis of the Escherichia coli Alp Phenotype: Heat Shock Induction in ssrA Mutants. J. Bacteriol. 187: 4739-4751 [Abstract] [Full Text]  
  • Kuo, M.-S., Chen, K.-P., Wu, W. F. (2004). Regulation of RcsA by the ClpYQ (HslUV) protease in Escherichia coli. Microbiology 150: 437-446 [Abstract] [Full Text]  
  • Pan, Q., Losick, R. (2003). Unique Degradation Signal for ClpCP in Bacillus subtilis. J. Bacteriol. 185: 5275-5278 [Abstract] [Full Text]  
  • Lee, Y.-Y., Chang, C.-F., Kuo, C.-L., Chen, M.-C., Yu, C. H., Lin, P.-I, Wu, W. F. (2003). Subunit Oligomerization and Substrate Recognition of the Escherichia coli ClpYQ (HslUV) Protease Implicated by In Vivo Protein-Protein Interactions in the Yeast Two-Hybrid System. J. Bacteriol. 185: 2393-2401 [Abstract] [Full Text]  
  • Couvreur, B., Wattiez, R., Bollen, A., Falmagne, P., Le Ray, D., Dujardin, J.-C. (2002). Eubacterial HslV and HslU Subunits Homologs in Primordial Eukaryotes. Mol Biol Evol 19: 2110-2117 [Abstract] [Full Text]  
  • Kuroda, A., Nomura, K., Ohtomo, R., Kato, J., Ikeda, T., Takiguchi, N., Ohtake, H., Kornberg, A. (2001). Role of Inorganic Polyphosphate in Promoting Ribosomal Protein Degradation by the Lon Protease in E. coli. Science 293: 705-708 [Abstract] [Full Text]  
  • Zhu, J., Winans, S. C. (2001). The quorum-sensing transcriptional regulator TraR requires its cognate signaling ligand for protein folding, protease resistance, and dimerization. Proc. Natl. Acad. Sci. USA 98: 1507-1512 [Abstract] [Full Text]  
  • SaiSree, L., Reddy, M., Gowrishankar, J. (2000). lon Incompatibility Associated with Mutations Causing SOS Induction: Null uvrD Alleles Induce an SOS Response in Escherichia coli. J. Bacteriol. 182: 3151-3157 [Abstract] [Full Text]  
  • Kanemori, M., Yanagi, H., Yura, T. (1999). Marked Instability of the sigma 32 Heat Shock Transcription Factor at High Temperature. IMPLICATIONS FOR HEAT SHOCK REGULATION. J. Biol. Chem. 274: 22002-22007 [Abstract] [Full Text]  
  • Wu, W.-F., Zhou, Y., Gottesman, S. (1999). Redundant In Vivo Proteolytic Activities of Escherichia coli Lon and the ClpYQ (HslUV) Protease. J. Bacteriol. 181: 3681-3687 [Abstract] [Full Text]  
  • Guzman-Verri, C., Chaves-Olarte, E., Garcia, F., Arvidson, S., Moreno, E. (2001). In Vivo Proteolytic Degradation of the Escherichia coli Acyltransferase HlyC. J. Biol. Chem. 276: 16660-16666 [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»