This Article Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Qu, J. N. Articles by Matsuzawa, H. Search for Related Content PubMed PubMed Citation Articles by Qu, J. N. Articles by Matsuzawa, H.

 Previous Article  |  Next Article 

J. Bacteriol., Jun 1996, 3457-3461, Vol 178, No. 12
Copyright © 1996, American Society for Microbiology

The tolZ gene of Escherichia coli is identified as the ftsH gene

JN Qu, SI Makino, H Adachi, Y Koyama, Y Akiyama, K Ito, T Tomoyasu, T Ogura and H Matsuzawa
Department of Biotechnology, University of Tokyo, Japan.

Escherichia coli tolZ mutants are tolerant to colicins E2, E3, D, Ia, and Ib (Tol-), can grow on glucose but not on succinate or other nonfermentable carbon sources (Nfc-), and show temperature-sensitive growth (Ts). A 1.8-kb DNA fragment that complemented the tolZ mutation was cloned. The DNA fragment was sequenced, and one open reading frame was found. This frame was identical to a part of the E. coli FtsH protein, an ATP-dependent metalloprotease that binds to the cytoplasmic membrane. The tolZ gene was located at 69 min on the E. coli genetic map, and the mutation was complemented by a plasmid carrying the ftsH gene, indicating that the tolZ gene is identical to the ftsH gene. The mutated tolZ21 gene was also cloned and sequenced and was found to have a single base change that caused an amino acid alteration of His-418 to Tyr in the FtsH protein. The tolZ21 mutant showed Hfl- (high frequency of lysogenization) and Std- (stop transfer-defective) pheno-types, both of which are due to a mutation in the ftsH (hflB) gene. However, the ftsH1, ftsH101, and hflB29 mutants did not show Tol- and Nfc phenotypes. The tolZ21 mutant was found to have a suppressor mutation, named sfhC, which allowed cells to survive. The sfhC mutation alone caused no Tol-, Nfc-, Ts, or Hfl- phenotypes in the tolZ21 mutant.

This article has been cited by other articles:

• Walker, D., Mosbahi, K., Vankemmelbeke, M., James, R., Kleanthous, C. (2007). The Role of Electrostatics in Colicin Nuclease Domain Translocation into Bacterial Cells. J. Biol. Chem. 282: 31389-31397 [Abstract] [Full Text]  
• Nagashima, K., Kubota, Y., Shibata, T., Sakaguchi, C., Shinagawa, H., Hishida, T. (2006). Degradation of Escherichia coli RecN Aggregates by ClpXP Protease and Its Implications for DNA Damage Tolerance. J. Biol. Chem. 281: 30941-30946 [Abstract] [Full Text]  
• Sze, C. C., Bernardo, L. M. D., Shingler, V. (2002). Integration of Global Regulation of Two Aromatic-Responsive {sigma}54-Dependent Systems: a Common Phenotype by Different Mechanisms. J. Bacteriol. 184: 760-770 [Abstract] [Full Text]  
• Shotland, Y., Shifrin, A., Ziv, T., Teff, D., Koby, S., Kobiler, O., Oppenheim, A. B. (2000). Proteolysis of Bacteriophage lambda CII by Escherichia coli FtsH (HflB). J. Bacteriol. 182: 3111-3116 [Abstract] [Full Text]  
• Karata, K., Inagawa, T., Wilkinson, A. J., Tatsuta, T., Ogura, T. (1999). Dissecting the Role of a Conserved Motif (the Second Region of Homology) in the AAA Family of ATPases. SITE-DIRECTED MUTAGENESIS OF THE ATP-DEPENDENT PROTEASE FtsH. J. Biol. Chem. 274: 26225-26232 [Abstract] [Full Text]  
• Bohn, C., Bouloc, P. (1998). The Escherichia coli cmlA Gene Encodes the Multidrug Efflux Pump Cmr/MdfA and Is Responsible for Isopropyl-beta -D-Thiogalactopyranoside Exclusion and Spectinomycin Sensitivity. J. Bacteriol. 180: 6072-6075 [Abstract] [Full Text]  
• Berlyn, M. K. B. (1998). Linkage Map of Escherichia coli K-12, Edition 10: The Traditional Map. Microbiol. Mol. Biol. Rev. 62: 814-984 [Abstract] [Full Text]  
• Akiyama, Y., Kihara, A., Mori, H., Ogura, T., Ito, K. (1998). Roles of the Periplasmic Domain of Escherichia coli FtsH (HflB) in Protein Interactions and Activity Modulation. J. Biol. Chem. 273: 22326-22333 [Abstract] [Full Text]