Journal of Bacteriology, October 2003, p. 5714-5721, Vol. 185, No. 19
0021-9193/03/$08.00+0 DOI: 10.1128/JB.185.19.5714-5721.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
RelA Is a Component of the Nutritional Stress Activation Pathway of the Bacillus subtilis Transcription Factor
B
Shuyu Zhang and W. G. Haldenwang*
Department of Microbiology and Immunology, University of Texas Health Science Center, San Antonio, Texas 78229-3900
Received 6 March 2003/
Accepted 3 July 2003
The general stress regulon of Bacillus subtilis is induced by the activation of the
B transcription factor. Activation of
B occurs when one of two phosphatases (RsbU and RsbP), each responding to a unique type of stress, actuates a positive regulator of
B by dephosphorylation. Nutritional stress triggers the RsbP phosphatase. The mechanism by which RsbP becomes active is unknown; however, its activation coincides with culture conditions that are likely to reduce the cell's levels of high-energy nucleotides. We now present evidence that RelA, a (p)ppGpp synthetase and the key enzyme of the stringent response, plays a role in nutritional stress activation of
B. An insertion mutation that disrupts relA blocks the activation of
B in response to PO4 or glucose limitation and inhibits the drop in ATP/GTP levels that normally accompanies
B induction under these conditions. In contrast, the activation of
B by physical stress (e.g., ethanol treatment) is not affected by the loss of RelA. RelA's role in
B activation appears to be distinct from its participation in the stringent response. Amino acid analogs which induce the stringent response and RelA-dependent (p)ppGpp synthesis do not trigger
B activity. In addition, neither a missense mutation in relA (relA240GE) nor a null mutation in rplK (rplK54), either of which is sufficient to inhibit the stringent response and RelA-dependent (p)ppGpp synthesis, fails to block
B activation by PO4 or glucose limitation.
* Corresponding author. Mailing address: Department of Microbiology & Immunology, MSC 7758, The University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX 78229-3900. Phone: (210) 567-3957. Fax: (210) 567-6612. E-mail: haldenwang{at}uthscsa.edu.
Journal of Bacteriology, October 2003, p. 5714-5721, Vol. 185, No. 19
0021-9193/03/$08.00+0 DOI: 10.1128/JB.185.19.5714-5721.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
This article has been cited by other articles:
-
Reeves, A., Haldenwang, W. G.
(2007). Isolation and Characterization of Dominant Mutations in the Bacillus subtilis Stressosome Components RsbR and RsbS. J. Bacteriol.
189: 1531-1541
[Abstract]
[Full Text]
-
Delumeau, O., Chen, C.-C., Murray, J. W., Yudkin, M. D., Lewis, R. J.
(2006). High-Molecular-Weight Complexes of RsbR and Paralogues in the Environmental Signaling Pathway of Bacillus subtilis. J. Bacteriol.
188: 7885-7892
[Abstract]
[Full Text]
-
Senn, M. M., Giachino, P., Homerova, D., Steinhuber, A., Strassner, J., Kormanec, J., Fluckiger, U., Berger-Bachi, B., Bischoff, M.
(2005). Molecular Analysis and Organization of the {sigma}B Operon in Staphylococcus aureus. J. Bacteriol.
187: 8006-8019
[Abstract]
[Full Text]
-
Zhang, S., Haldenwang, W. G.
(2005). Contributions of ATP, GTP, and Redox State to Nutritional Stress Activation of the Bacillus subtilis {sigma}B Transcription Factor. J. Bacteriol.
187: 7554-7560
[Abstract]
[Full Text]
-
Kaneko, T., Tanaka, N., Kumasaka, T.
(2005). Crystal structures of RsbQ, a stress-response regulator in Bacillus subtilis. Protein Sci.
14: 558-565
[Abstract]
[Full Text]
-
Kuo, S., Zhang, S., Woodbury, R. L., Haldenwang, W. G.
(2004). Associations between Bacillus subtilis {sigma}B regulators in cell extracts. Microbiology
150: 4125-4136
[Abstract]
[Full Text]
-
Chen, C.-C., Yudkin, M. D., Delumeau, O.
(2004). Phosphorylation and RsbX-Dependent Dephosphorylation of RsbR in the RsbR-RsbS Complex of Bacillus subtilis. J. Bacteriol.
186: 6830-6836
[Abstract]
[Full Text]
-
Chaturongakul, S., Boor, K. J.
(2004). RsbT and RsbV Contribute to {sigma}B-Dependent Survival under Environmental, Energy, and Intracellular Stress Conditions in Listeria monocytogenes. Appl. Environ. Microbiol.
70: 5349-5356
[Abstract]
[Full Text]
-
Wout, P., Pu, K., Sullivan, S. M., Reese, V., Zhou, S., Lin, B., Maddock, J. R.
(2004). The Escherichia coli GTPase CgtAE Cofractionates with the 50S Ribosomal Subunit and Interacts with SpoT, a ppGpp Synthetase/Hydrolase. J. Bacteriol.
186: 5249-5257
[Abstract]
[Full Text]
-
Woodbury, R. L., Luo, T., Grant, L., Haldenwang, W. G.
(2004). Mutational Analysis of RsbT, an Activator of the Bacillus subtilis Stress Response Transcription Factor, {sigma}B. J. Bacteriol.
186: 2789-2797
[Abstract]
[Full Text]
Copyright © 2003 by the American Society for Microbiology. All rights reserved.