This Article
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 Iuchi, S
Right arrow Articles by Lin, E C
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Iuchi, S
Right arrow Articles by Lin, E C

 Previous Article  |  Next Article 

J Bacteriol. 1992 September; 174(17): 5617-5623

research-article

Purification and phosphorylation of the Arc regulatory components of Escherichia coli.

S Iuchi and E C Lin

Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115.

ABSTRACT

In Escherichia coli, a two-component signal transduction system, consisting of the transmembrane sensor protein ArcB and its cognate cytoplasmic regulatory protein ArcA, controls the expression of genes encoding enzymes involved in aerobic respiration. ArcB belongs to a subclass of sensors that have not only a conserved histidine-containing transmitter domain but also a conserved aspartate-containing receiver domain of the regulator family. 'ArcB (a genetically truncated ArcB missing the two transmembrane segments on the N-terminal end) and ArcA were purified from overproducing cells. Autophosphorylation of 'ArcB was revealed when the protein was incubated with [gamma-32P]ATP but not with [alpha-32P]ATP or [gamma-32P]GTP. When ArcA was incubated in the presence of 'ArcB and [gamma-32P]ATP, ArcA acquired radioactivity at the expense of the phosphorylated protein 'ArcB-32P. When a limited amount of 'ArcB was incubated with excess ArcA and [gamma-32P]ATP, ArcA-32P increased linearly with time. Under such conditions, for a given time period the amount of ArcA phosphorylated was proportional to the concentration of 'ArcB. Thus, 'ArcB acted as a kinase for ArcA. Chemical stabilities of the phosphorylated proteins suggested that 'ArcB-32P contained both a histidyl phosphate and an aspartyl phosphate(s) and that ArcA-32P contained only an aspartyl phosphate(s).

J Bacteriol. 1992 September; 174(17): 5617-5623




This article has been cited by other articles:

  • Wang, X., Gao, H., Shen, Y., Weinstock, G. M., Zhou, J., Palzkill, T. (2008). A high-throughput percentage-of-binding strategy to measure binding energies in DNA-protein interactions: application to genome-scale site discovery. Nucleic Acids Res 36: 4863-4871 [Abstract] [Full Text]  
  • Cho, B.-K., Knight, E. M., Palsson, B. O. (2006). Transcriptional regulation of the fad regulon genes of Escherichia coli by ArcA.. Microbiology 152: 2207-2219 [Abstract] [Full Text]  
  • Yamamoto, K., Hirao, K., Oshima, T., Aiba, H., Utsumi, R., Ishihama, A. (2005). Functional Characterization in Vitro of All Two-component Signal Transduction Systems from Escherichia coli. J. Biol. Chem. 280: 1448-1456 [Abstract] [Full Text]  
  • Zhou, R., Wolk, C. P. (2003). A Two-component System Mediates Developmental Regulation of Biosynthesis of a Heterocyst Polysaccharide. J. Biol. Chem. 278: 19939-19946 [Abstract] [Full Text]  
  • Georgellis, D., Kwon, O., Lin, E. C. C., Wong, S. M., Akerley, B. J. (2001). Redox Signal Transduction by the ArcB Sensor Kinase of Haemophilus influenzae Lacking the PAS Domain. J. Bacteriol. 183: 7206-7212 [Abstract] [Full Text]  
  • Alexeeva, S., de Kort, B., Sawers, G., Hellingwerf, K. J., de Mattos, M. J. T. (2000). Effects of Limited Aeration and of the ArcAB System on Intermediary Pyruvate Catabolism in Escherichia coli. J. Bacteriol. 182: 4934-4940 [Abstract] [Full Text]  
  • Georgellis, D., Kwon, O., De Wulf, P., Lin, E. C. C. (1998). Signal Decay through a Reverse Phosphorelay in the Arc Two-component Signal Transduction System. J. Biol. Chem. 273: 32864-32869 [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]  
  • Matsushika, A., Mizuno, T. (1998). A Dual-Signaling Mechanism Mediated by the ArcB Hybrid Sensor Kinase Containing the Histidine-Containing Phosphotransfer Domain in Escherichia coli. J. Bacteriol. 180: 3973-3977 [Abstract] [Full Text]  
  • Ma, S., Wozniak, D. J., Ohman, D. E. (1997). Identification of the Histidine Protein Kinase KinB in Pseudomonas aeruginosa and Its Phosphorylation of the Alginate Regulator AlgB. J. Biol. Chem. 272: 17952-17960 [Abstract] [Full Text]  
  • Mushegian, A. R., Bassett, D. E. Jr., Boguski, M. S., Bork, P., Koonin, E. V. (1997). Positionally cloned human disease genes: Patterns of evolutionary conservation and functional motifs. Proc. Natl. Acad. Sci. USA 94: 5831-5836 [Abstract] [Full Text]  
  • Uhl, M. A., Miller, J. F. (1996). Central Role of the BvgS Receiver as a Phosphorylated Intermediate in a Complex Two-component Phosphorelay. J. Biol. Chem. 271: 33176-33180 [Abstract] [Full Text]  
  • Pernestig, A.-K., Melefors, O., Georgellis, D. (2001). Identification of UvrY as the Cognate Response Regulator for the BarA Sensor Kinase in Escherichia coli. J. Biol. Chem. 276: 225-231 [Abstract] [Full Text]  
  • Lee, Y. S., Han, J. S., Jeon, Y., Hwang, D. S. (2001). The Arc Two-component Signal Transduction System Inhibits in Vitro Escherichia coli Chromosomal Initiation. J. Biol. Chem. 276: 9917-9923 [Abstract] [Full Text]  
  • Jeon, Y., Lee, Y. S., Han, J. S., Kim, J. B., Hwang, D. S. (2001). Multimerization of Phosphorylated and Non-phosphorylated ArcA Is Necessary for the Response Regulator Function of the Arc Two-component Signal Transduction System. J. Biol. Chem. 276: 40873-40879 [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»