Architecture of the complete oxygen-sensing FixL-FixJ two-component signal transduction system

2018 ◽  
Vol 11 (525) ◽  
pp. eaaq0825 ◽  
Author(s):  
Gareth S. A. Wright ◽  
Akane Saeki ◽  
Takaaki Hikima ◽  
Yoko Nishizono ◽  
Tamao Hisano ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Oxygen Sensing ◽  
Signal Transduction System ◽  
Two Component ◽  
Two Component Signal Transduction

Phosphorylation activity of the response regulator of the two-component signal transduction system AtoS–AtoC in E. coli

2005 ◽  
Vol 1725 (3) ◽  
pp. 257-268 ◽  
Author(s):  
Efthimia E. Lioliou ◽  
Eleni P. Mimitou ◽  
Asterios I. Grigoroudis ◽  
Cynthia H. Panagiotidis ◽  
Christos A. Panagiotidis ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Response Regulator ◽  
Signal Transduction System ◽  
E Coli ◽  
Two Component ◽  
Two Component Signal Transduction

scholarly journals CheX in the Three-Phosphatase System of Bacterial Chemotaxis

2007 ◽  
Vol 189 (19) ◽  
pp. 7007-7013 ◽  
Author(s):  
Travis J. Muff ◽  
Richard M. Foster ◽  
Peter J. Y. Liu ◽  
George W. Ordal
Keyword(s):  
Escherichia Coli ◽  
Signal Transduction ◽  
Bacillus Subtilis ◽  
Mutant Strain ◽  
Response Regulator ◽  
Bacterial Chemotaxis ◽  
Signal Transduction System ◽  
Two Component ◽  
Two Component Signal Transduction ◽  
Phosphatase System

ABSTRACT Bacterial chemotaxis involves the regulation of motility by a modified two-component signal transduction system. In Escherichia coli, CheZ is the phosphatase of the response regulator CheY but many other bacteria, including Bacillus subtilis, use members of the CheC-FliY-CheX family for this purpose. While Bacillus subtilis has only CheC and FliY, many systems also have CheX. The effect of this three-phosphatase system on chemotaxis has not been studied previously. CheX was shown to be a stronger CheY-P phosphatase than either CheC or FliY. In Bacillus subtilis, a cheC mutant strain was nearly complemented by heterologous cheX expression. CheX was shown to overcome the ΔcheC adaptational defect but also generally lowered the counterclockwise flagellar rotational bias. The effect on rotational bias suggests that CheX reduced the overall levels of CheY-P in the cell and did not truly replicate the adaptational effects of CheC. Thus, CheX is not functionally redundant to CheC and, as outlined in the discussion, may be more analogous to CheZ.

scholarly journals Autoregulation of Lantibiotic Bovicin HJ50 Biosynthesis by the BovK-BovR Two-Component Signal Transduction System inStreptococcus bovisHJ50

2010 ◽  
Vol 77 (2) ◽  
pp. 407-415 ◽  
Author(s):  
Jianqiang Ni ◽  
Kunling Teng ◽  
Gang Liu ◽  
Caixia Qiao ◽  
Liandong Huan ◽  
...  
Keyword(s):  
Gene Expression ◽  
Signal Transduction ◽  
Fluorescent Protein ◽  
Specific Binding ◽  
Biosynthetic Gene Cluster ◽  
Phosphoryl Group ◽  
Signal Transduction System ◽  
Two Component ◽  
Two Component Signal Transduction ◽  
Green Fluorescent

ABSTRACTStreptococcus bovisHJ50 produces a lacticin 481-like 33-amino-acid-residue lantibiotic, designated bovicin HJ50.bovK-bovRin the bovicin HJ50 biosynthetic gene cluster is predicted to be a two-component signal transduction system involved in sensing signals and regulating gene expression. Disruption ofbovKorbovRresulted in the abrogation of bovicin HJ50 production, suggesting both genes play important roles in bovicin HJ50 biosynthesis. Addition of exogenous bovicin HJ50 peptide to cultures of abovMmutant that lost the capability for bovicin HJ50 production and structural genebovAtranscription inS. bovisHJ50 induced dose-dependent transcription of thebovAgene, demonstrating that bovicin HJ50 production was normally autoregulated. The transcription ofbovAwas no longer induced by bovicin HJ50 inbovKandbovRdisruption mutants, suggesting that BovK-BovR plays an essential role in the signal transduction regulating bovicin HJ50 biosynthesis. A phosphorylation assay indicated that BovK has the ability to autophosphorylate and subsequently transfer the phosphoryl group to the downstream BovR protein to carry on signal transduction. Electromobility shift assays (EMSA) and green fluorescent protein (GFP) reporter gene expression assays showed the specific binding of BovR to thebovApromoter, indicating that BovR regulatesbovAexpression by direct binding between them. Taken together, bovicin HJ50 biosynthesis is induced by bovicin HJ50 itself and regulated via the two-component signal transduction system BovK-BovR.

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