scholarly journals A Two-component Signal Transduction Pathway Regulates Manganese Homeostasis inSynechocystis6803, a Photosynthetic Organism

2002 ◽  
Vol 277 (32) ◽  
pp. 28981-28986 ◽  
Author(s):  
Teruo Ogawa ◽  
Ding Hui Bao ◽  
Hirokazu Katoh ◽  
Mari Shibata ◽  
Himadri B. Pakrasi ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Signal Transduction Pathway ◽  
Transduction Pathway ◽  
Two Component ◽  
Photosynthetic Organism ◽  
Two Component Signal Transduction

scholarly journals P Pilus Assembly Motif Necessary for Activation of the CpxRA Pathway by PapE in Escherichia coli

2004 ◽  
Vol 186 (13) ◽  
pp. 4326-4337 ◽  
Author(s):  
Yvonne M. Lee ◽  
Patricia A. DiGiuseppe ◽  
Thomas J. Silhavy ◽  
Scott J. Hultgren
Keyword(s):  
Escherichia Coli ◽  
Signal Transduction ◽  
Signal Transduction Pathway ◽  
The Self ◽  
Carboxyl Terminus ◽  
Transduction Pathway ◽  
Two Component ◽  
Pilus Biogenesis ◽  
Two Component Signal Transduction ◽  
Self Association

ABSTRACT P pilus biogenesis occurs via the highly conserved chaperone-usher pathway, and assembly is monitored by the CpxRA two-component signal transduction pathway. Structural pilus subunits consist of an N-terminal extension followed by an incomplete immunoglobulin-like fold that is missing a C-terminal seventh beta strand. In the pilus fiber, the immunoglobulin-like fold of each pilin is completed by the N-terminal extension of its neighbor. Subunits that do not get incorporated into the pilus fiber are driven “OFF-pathway.” In this study, we found that PapE was the only OFF-pathway nonadhesin P pilus subunit capable of activating Cpx. Manipulation of the PapE structure by removing, relocating within the protein, or swapping its N-terminal extension with that of other subunits altered the protein's self-associative and Cpx-activating properties. The self-association properties of the new subunits were dictated by the specific N-terminal extension provided and were consistent with the order of the subunits in the pilus fiber. However, these aggregation properties did not directly correlate with Cpx induction. Cpx activation instead correlated with the presence or absence of an N-terminal extension in the PapE pilin structure. Removal of the N-terminal extension of PapE was sufficient to abolish Cpx activation. Replacement of an N-terminal extension at either the amino or carboxyl terminus restored Cpx induction. Thus, the data presented in this study argue that PapE has features inherent in its structure or during its folding that act as specific inducers of Cpx signal transduction.

scholarly journals Dissecting the VanRS Signal Transduction Pathway with Specific Inhibitors

1999 ◽  
Vol 181 (2) ◽  
pp. 627-631 ◽  
Author(s):  
Andrew T. Ulijasz ◽  
Bernard Weisblum
Keyword(s):  
Signal Transduction ◽  
Pseudomonas Aeruginosa ◽  
Transcriptional Activation ◽  
Signal Transduction Pathway ◽  
Phosphoryl Transfer ◽  
Transduction Pathway ◽  
Two Component ◽  
Two Component Signal Transduction ◽  
Specific Inhibitors

ABSTRACT The VanRS two-component signal transduction pathway fromEnterococcus faecium was reconstituted in vitro from partially purified components and shown to be inhibited by the halophenyl isothiazolone LY-266,400, inhibitor A, a compound shown previously to reduce expression of the AlgR1-AlgR2 two-component signal transduction pathway in Pseudomonas aeruginosa (S. Roychoudhury, N. A. Zielinski, A. J. Ninfa, N. E. Allen, L. N. Jungheim, T. I. Nicas, and A. M. Chakrabarty, Proc. Natl. Acad. Sci. USA 90:965–969, 1993). Inhibitor A attenuates phosphoryl transfer from VanS∼P to VanR by its action on the ability of VanR to accept. We observed an apparent stimulatory effect of inhibitor A on VanS autophosphorylation which is attributable to the accumulation of VanS∼P as an intermediate unable to transfer Pi to the inhibited VanR. Thus, inhibitor A acts on the second of two sequential steps which lead to transcriptional activation of the VanHAXYZ gene cluster and the resultant expression of vancomycin resistance.

scholarly journals A Novel Two-Component System, GluR-GluK, Involved in Glutamate Sensing and Uptake in Streptomyces coelicolor

2017 ◽  
Vol 199 (18) ◽  
Author(s):  
Lei Li ◽  
Weihong Jiang ◽  
Yinhua Lu
Keyword(s):  
Signal Transduction ◽  
Glutamate Uptake ◽  
Streptomyces Coelicolor ◽  
Signal Transduction Pathway ◽  
Antibiotic Biosynthesis ◽  
Transduction Pathway ◽  
Two Component System ◽  
Component System ◽  
Content Type ◽  
Two Component

ABSTRACT Two-component systems (TCSs), the predominant signal transduction pathways employed by bacteria, play important roles in physiological metabolism in Streptomyces. Here, a novel TCS, GluR-GluK (encoded by SCO5778-SCO5779), which is located divergently from the gluABCD operon encoding a glutamate uptake system, was identified as being involved in glutamate sensing and uptake as well as antibiotic biosynthesis in Streptomyces coelicolor. Under the condition of minimal medium (MM) supplemented with different concentrations of glutamate, deletion of the gluR-gluK operon (gluR-K) resulted in enhanced actinorhodin (ACT) but reduced undecylprodigiosin (RED) and yellow type I polyketide (yCPK) production, suggesting that GluR-GluK plays a differential role in antibiotic biosynthesis. Furthermore, we found that the response regulator GluR directly promotes the expression of gluABCD under the culture condition of MM with a high concentration of glutamate (75 mM). Using the biolayer interferometry assay, we demonstrated that glutamate acts as the direct signal of the histidine kinase GluK. It was therefore suggested that upon sensing high concentrations of glutamate, GluR-GluK would be activated and thereby facilitate glutamate uptake by increasing gluABCD expression. Finally, we demonstrated that the role of GluR-GluK in antibiotic biosynthesis is independent of its function in glutamate uptake. Considering the wide distribution of the glutamate-sensing (GluR-GluK) and uptake (GluABCD) module in actinobacteria, it could be concluded that the GluR-GluK signal transduction pathway involved in secondary metabolism and glutamate uptake should be highly conserved in this bacterial phylum. IMPORTANCE In this study, a novel two-component system (TCS), GluR-GluK, was identified to be involved in glutamate sensing and uptake as well as antibiotic biosynthesis in Streptomyces coelicolor. A possible GluR-GluK working model was proposed. Upon sensing high glutamate concentrations (such as 75 mM), activated GluR-GluK could regulate both glutamate uptake and antibiotic biosynthesis. However, under a culture condition of MM supplemented with low concentrations of glutamate (such as 10 mM), although GluR-GluK is activated, its activity is sufficient only for the regulation of antibiotic biosynthesis. To the best of our knowledge, this is the first report describing a TCS signal transduction pathway for glutamate sensing and uptake in actinobacteria.

scholarly journals The Two-Component Signal Transduction Protein Chk1p Regulates Quorum Sensing in Candida albicans

2004 ◽  
Vol 3 (4) ◽  
pp. 1062-1065 ◽  
Author(s):  
Michael Kruppa ◽  
Bastiaan P. Krom ◽  
Neeraj Chauhan ◽  
Adrienne V. Bambach ◽  
Ronald L. Cihlar ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Candida Albicans ◽  
Quorum Sensing ◽  
Signal Transduction Pathway ◽  
Inhibitory Effect ◽  
Signal Transduction Protein ◽  
Hyphal Morphogenesis ◽  
Eukaryotic Organism ◽  
Two Component ◽  
Two Component Signal Transduction

ABSTRACT Regulation of hyphal morphogenesis in Candida albicans can occur through quorum sensing (QS). A QS signal, farnesol, is produced during high-density growth and inhibits morphogenesis. However, the signal transduction pathway that regulates QS is unknown. Here, we show that a C. albicans mutant lacking Chk1p but not either the Sln1p or the Nik1p histidine kinase is refractory to the inhibitory effect of farnesol both in cell suspension and during the formation of a biofilm. This study is the first to demonstrate a role for a two-component signal transduction protein in QS by a eukaryotic organism.

scholarly journals Histidine Phosphotransfer Proteins in Fungal Two-Component Signal Transduction Pathways

2013 ◽  
Vol 12 (8) ◽  
pp. 1052-1060 ◽  
Author(s):  
Jan S. Fassler ◽  
Ann H. West
Keyword(s):  
Signal Transduction ◽  
Response Regulator ◽  
Single Gene ◽  
Signal Transduction Pathway ◽  
Pathogenic Fungi ◽  
Kinase Gene ◽  
Content Type ◽  
Two Component ◽  
Two Component Signal Transduction ◽  
Histidine Phosphotransfer

ABSTRACTThe histidine phosphotransfer (HPt) protein Ypd1 is an important participant in theSaccharomyces cerevisiaemultistep two-component signal transduction pathway and, unlike the expanded histidine kinase gene family, is encoded by a single gene in nearly all model and pathogenic fungi. Ypd1 is essential for viability in bothS. cerevisiaeand inCryptococcus neoformans. These and other aspects of Ypd1 biology, combined with the availability of structural and mutational data inS. cerevisiae, suggest that the essential interactions between Ypd1 and response regulator domains would be a good target for antifungal drug development. The goal of this minireview is to summarize the wealth of data onS. cerevisiaeYpd1 and to consider the potential benefits of conducting related studies in pathogenic fungi.

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