This Article Full Text (PDF) 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 Lin, Y P Articles by March, P E Search for Related Content PubMed PubMed Citation Articles by Lin, Y P Articles by March, P E

 Previous Article  |  Next Article 

J Bacteriol. 1994 January; 176(1): 44-49

research-article

GTPase-dependent signaling in bacteria: characterization of a membrane-binding site for era in Escherichia coli.

Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway 08854-5635.

ABSTRACT

Era is an Escherichia coli GTPase that is essential for cell viability and is peripherally associated with the cytoplasmic membrane. Both immunoelectron microscopy and subcellular-fractionation experiments have shown that Era is present in cytoplasmic as well as membrane-associated pools. These data led to speculation that the mechanism of action of Era may require cycling between membrane and cytoplasmic sites. In order to investigate this possibility, an in vitro binding assay was developed to characterize the binding of Era to membrane fractions. Competition and saturation binding experiments suggest that a site that is specific for Era and capable of binding up to 5 ng of Era per microgram of membrane protein is present in membrane preparations. The binding curve is complex, indicating that multiple equilibria describe the interaction. The binding of Era to this putative receptor is dependent on guanine nucleotides; binding cannot be measured in the absence of nucleotide, and neither ATP nor UTP can substitute. Subfractionation of cell walls showed that the guanine nucleotide-dependent binding site was present in fractions enriched in cytoplasmic membrane. These data provide evidence that Era may be involved in a GTPase-receptor-coupled membrane-signaling pathway that is essential for growth in E. coli.

This article has been cited by other articles:

• Ohk, S.-H., Kuramitsu, H. K. (2000). A novel antibacterial agent derived from the C-terminal domain of Streptococcus mutans GTP-binding protein. J Antimicrob Chemother 46: 95-99 [Abstract] [Full Text]  
• Meier, T. I., Peery, R. B., McAllister, K. A., Zhao, G. (2000). Era GTPase of Escherichia coli: binding to 16S rRNA and modulation of GTPase activity by RNA and carbohydrates. Microbiology 146: 1071-1083 [Abstract] [Full Text]  
• Mehr, I. J., Long, C. D., Serkin, C. D., Seifert, H. S. (2000). A Homologue of the Recombination-Dependent Growth Gene, rdgC, Is Involved in Gonococcal Pilin Antigenic Variation. Genetics 154: 523-532 [Abstract] [Full Text]  
• Bruser, T., Selmer, T., Dahl, C. (2000). "ADP Sulfurylase" from Thiobacillus denitrificans Is an Adenylylsulfate:Phosphate Adenylyltransferase and Belongs to a New Family of Nucleotidyltransferases. J. Biol. Chem. 275: 1691-1698 [Abstract] [Full Text]  
• Kuzminov, A. (1999). Recombinational Repair of DNA Damage in Escherichia coli and Bacteriophage lambda. Microbiol. Mol. Biol. Rev. 63: 751-813 [Abstract] [Full Text]  
• Baev, D., England, R., Kuramitsu, H. K. (1999). Stress-Induced Membrane Association of the Streptococcus mutans GTP-Binding Protein, an Essential G Protein, and Investigation of Its Physiological Role by Utilizing an Antisense RNA Strategy. Infect. Immun. 67: 4510-4516 [Abstract] [Full Text]  
• Meier, T. I., Peery, R. B., Jaskunas, S. R., Zhao, G. (1999). 16S rRNA Is Bound to Era of Streptococcus pneumoniae. J. Bacteriol. 181: 5242-5249 [Abstract] [Full Text]  
• Lu, Q., Inouye, M. (1998). The Gene for 16S rRNA Methyltransferase (ksgA) Functions as a Multicopy Suppressor for a Cold-Sensitive Mutant of Era, an Essential RAS-Like GTP-Binding Protein in Escherichia coli. J. Bacteriol. 180: 5243-5246 [Abstract] [Full Text]