HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Georgellis, D. Articles by Lin, E. C. C. Search for Related Content PubMed PubMed Citation Articles by Georgellis, D. Articles by Lin, E. C. C. Social Bookmarking                      What's this?

J Biol Chem, Vol. 274, Issue 50, 35950-35954, December 10, 1999

Amplification of Signaling Activity of the Arc Two-component System of Escherichia coli by Anaerobic Metabolites
AN IN VITRO STUDY WITH DIFFERENT PROTEIN MODULES^*

Dimitris Georgellis, Ohsuk Kwon, and Edmund C. C. Lin^§

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

In Escherichia coli, changes in redox condition of growth are sensed and signaled by the Arc two-component system. This system consists of ArcB as the membrane-associated sensor kinase and ArcA as the cytoplasmic response regulator. ArcB is a tripartite kinase, possessing a primary transmitter, a receiver, and a secondary transmitter domain that catalyzes the phosphorylation of ArcA via a His  Asp  His  Asp phosphorelay, as well as the dephosphorylation of ArcA-P by a reverse phosphorelay. When ArcA and ArcB were incubated with ATP, the peak levels of phosphorylated proteins increased in the presence of the fermentation metabolites D-lactate, acetate, or pyruvate. In this study, we report that these effectors accelerate the autophosphorylation activity of ArcB and enhance the transphosphorylation of ArcA, but have no effect on the dephosphorylation of ArcA-P. Moreover, the presence of the receiver domain of ArcB is essential for the effectors to influence the autophosphorylation rate of the primary transmitter domain of ArcB.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				J. D. Partridge, C. Scott, Y. Tang, R. K. Poole, and J. Green Escherichia coli Transcriptome Dynamics during the Transition from Anaerobic to Aerobic Conditions J. Biol. Chem., September 22, 2006; 281(38): 27806 - 27815. [Abstract] [Full Text] [PDF]

				M. B. Clarke, D. T. Hughes, C. Zhu, E. C. Boedeker, and V. Sperandio The QseC sensor kinase: A bacterial adrenergic receptor PNAS, July 5, 2006; 103(27): 10420 - 10425. [Abstract] [Full Text] [PDF]

				G. R. Pena-Sandoval, O. Kwon, and D. Georgellis Requirement of the Receiver and Phosphotransfer Domains of ArcB for Efficient Dephosphorylation of Phosphorylated ArcA In Vivo J. Bacteriol., May 1, 2005; 187(9): 3267 - 3272. [Abstract] [Full Text] [PDF]

				R. Malpica, B. Franco, C. Rodriguez, O. Kwon, and D. Georgellis Identification of a quinone-sensitive redox switch in the ArcB sensor kinase PNAS, September 7, 2004; 101(36): 13318 - 13323. [Abstract] [Full Text] [PDF]

				C. Rodriguez, O. Kwon, and D. Georgellis Effect of D-Lactate on the Physiological Activity of the ArcB Sensor Kinase in Escherichia coli J. Bacteriol., April 1, 2004; 186(7): 2085 - 2090. [Abstract] [Full Text] [PDF]

				D. K. Saini, V. Malhotra, D. Dey, N. Pant, T. K. Das, and J. S. Tyagi DevR-DevS is a bona fide two-component system of Mycobacterium tuberculosis that is hypoxia-responsive in the absence of the DNA-binding domain of DevR Microbiology, April 1, 2004; 150(4): 865 - 875. [Abstract] [Full Text] [PDF]

				O. Kwon, D. Georgellis, and E. C. C. Lin Rotational On-off Switching of a Hybrid Membrane Sensor Kinase Tar-ArcB in Escherichia coli J. Biol. Chem., April 4, 2003; 278(15): 13192 - 13195. [Abstract] [Full Text] [PDF]

				K. P. Fong, L. Gao, and D. R. Demuth luxS and arcB Control Aerobic Growth of Actinobacillus actinomycetemcomitans under Iron Limitation Infect. Immun., January 1, 2003; 71(1): 298 - 308. [Abstract] [Full Text] [PDF]

				I. G. Janausch, I. Garcia-Moreno, and G. Unden Function of DcuS from Escherichia coli as a Fumarate-stimulated Histidine Protein Kinase in Vitro J. Biol. Chem., October 11, 2002; 277(42): 39809 - 39814. [Abstract] [Full Text] [PDF]

				S. Lu, P. B. Killoran, F. C. Fang, and L. W. Riley The Global Regulator ArcA Controls Resistance to Reactive Nitrogen and Oxygen Intermediates in Salmonella enterica Serovar Enteritidis Infect. Immun., February 1, 2002; 70(2): 451 - 461. [Abstract] [Full Text] [PDF]

				R. B. Bourret, N. W. Charon, A. M. Stock, and A. H. West Bright Lights, Abundant Operons--Fluorescence and Genomic Technologies Advance Studies of Bacterial Locomotion and Signal Transduction: Review of the BLAST Meeting, Cuernavaca, Mexico, 14 to 19 January 2001 J. Bacteriol., January 1, 2002; 184(1): 1 - 17. [Full Text] [PDF]

				D. T. Verhamme, J. C. Arents, P. W. Postma, W. Crielaard, and K. J. Hellingwerf Investigation of in vivo cross-talk between key two-component systems of Escherichia coli Microbiology, January 1, 2002; 148(1): 69 - 78. [Abstract] [Full Text] [PDF]

				D. Georgellis, O. Kwon, E. C. C. Lin, S. M. Wong, and B. J. Akerley Redox Signal Transduction by the ArcB Sensor Kinase of Haemophilus influenzae Lacking the PAS Domain J. Bacteriol., December 15, 2001; 183(24): 7206 - 7212. [Abstract] [Full Text] [PDF]

				D. Georgellis, O. Kwon, and E. C. C. Lin Quinones as the Redox Signal for the Arc Two-Component System of Bacteria Science, June 22, 2001; 292(5525): 2314 - 2316. [Abstract] [Full Text] [PDF]

				O. Kwon, D. Georgellis, and E. C. C. Lin Phosphorelay as the Sole Physiological Route of Signal Transmission by the Arc Two-Component System of Escherichia coli J. Bacteriol., July 1, 2000; 182(13): 3858 - 3862. [Abstract] [Full Text]

				O. Kwon, D. Georgellis, A. S. Lynch, D. Boyd, and E. C. C. Lin The ArcB Sensor Kinase of Escherichia coli: Genetic Exploration of the Transmembrane Region J. Bacteriol., May 15, 2000; 182(10): 2960 - 2966. [Abstract] [Full Text]

				A.-K. Pernestig, O. Melefors, and D. Georgellis Identification of UvrY as the Cognate Response Regulator for the BarA Sensor Kinase in Escherichia coli J. Biol. Chem., January 5, 2001; 276(1): 225 - 231. [Abstract] [Full Text] [PDF]

				Y. Jeon, Y. S. Lee, J. S. Han, J. B. Kim, and D. S. Hwang 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., October 26, 2001; 276(44): 40873 - 40879. [Abstract] [Full Text] [PDF]