scholarly journals Improving Orthogonality in Two-Component Biological Signalling Systems Using Feedback Control

2019 ◽  
Vol 3 (2) ◽  
pp. 326-331 ◽  
Author(s):  
Harrison Steel ◽  
Aivar Sootla ◽  
Benjamin Smart ◽  
Nicolas Delalez ◽  
Antonis Papachristodoulou
2001 ◽  
Vol 356 (1415) ◽  
pp. 1745-1753 ◽  
Author(s):  
David E. Somers

The identification of components of the plant circadian clock has been advanced recently with the success of two forward genetics approaches. The ZEITLUPE and TOC1 loci were cloned and each was found to be part of two separate, larger gene families with intriguing domain structures. The ZTL family of proteins contains a subclass of the PAS domain coupled to an F box and kelch motifs, suggesting that they play a role in a novel light–regulated ubiquitination mechanism. TOC1 shares similarity to the receiver domain of the well–known two–component phosphorelay signalling systems, combined with a strong similarity to a region of the CONSTANS transcription factor, which is involved in controlling flowering time. When added to the repertoire of previously identified clock–associated genes, it is clear that both similarities and differences with other circadian systems will emerge in the coming years.


2019 ◽  
Author(s):  
Benjamin J. Stein ◽  
Aretha Fiebig ◽  
Sean Crosson

AbstractTwo-component signaling systems (TCSs) function to detect environmental cues and transduce this information into a change in transcription. In its simplest form, TCS-dependent regulation of transcription entails phosphoryl-transfer from a sensory histidine kinase to its cognate DNA-binding receiver protein. However, in certain cases, auxiliary proteins may modulate TCSs in response to secondary environmental cues. Caulobacter crescentus FixT is one such auxiliary regulator. FixT is composed of a single receiver domain and functions as a feedback inhibitor of the FixL-FixJ (FixLJ) TCS, which regulates the transcription of genes involved in adaptation to microaerobiosis. We sought to define the impact of fixT on Caulobacter cell physiology and to understand the molecular mechanism by which FixT represses FixLJ signaling. fixT deletion results in excess production of porphyrins and premature entry into stationary phase, demonstrating the importance of feedback inhibition of the FixLJ signaling system. Although FixT is a receiver domain, it does not affect dephosphorylation of the oxygen-sensor kinase FixL or phosphoryltransfer from FixL to its cognate receiver FixJ. Rather, FixT represses FixLJ signaling by inhibiting the FixL autophosphorylation reaction. We have further identified a 4-cysteine motif in Caulobacter FixT that binds an Fe-S cluster and protects the protein from degradation by the Lon protease. Our data support a model in which oxidation of this Fe-S cluster promotes degradation of FixT in vivo. This proteolytic mechanism facilitates clearance the of the FixT feedback inhibitor from the cell under normoxia and resets the FixLJ system for a future microaerobic signaling event.ImportanceTwo-component signal transduction systems (TCSs) are broadly conserved in the bacterial kingdom and generally contain two molecular components: a sensor histidine kinase and a receiver protein. Sensor histidine kinases alter their phosphorylation state in direct response to a physical or chemical cue, whereas receiver proteins “receive” the phosphoryl group from the kinase to regulate a change in cell physiology. We have discovered that a single-domain receiver protein, FixT, binds an Fe-S cluster and controls Caulobacter heme homeostasis though its function as a negative feedback regulator of the oxygen-sensor kinase, FixL. We provide evidence that the Fe-S cluster protects FixT from Lon-dependent proteolysis in the cell and endows FixT with the ability to function as a second, autonomous oxygen/redox sensor in the FixL-FixJ signaling pathway. This study introduces a novel mechanism of regulated TCS feedback control by an Fe-S-binding receiver domain.


2000 ◽  
Vol 9 (10) ◽  
pp. 2351-2369 ◽  
Author(s):  
Mark J Macielag ◽  
Raul Goldschmidt

2016 ◽  
pp. gkw642 ◽  
Author(s):  
Anaïs Brosse ◽  
Anna Korobeinikova ◽  
Susan Gottesman ◽  
Maude Guillier

2015 ◽  
Vol 469 (1) ◽  
pp. 121-134 ◽  
Author(s):  
Ruchi Agrawal ◽  
Akancha Pandey ◽  
Mayooreshwar P. Rajankar ◽  
Narendra M. Dixit ◽  
Deepak K. Saini

Bacteria use two-component signalling systems (TCSs) to sense and respond to environmental changes. Currently, they are thought to be highly specific, with each TCS functioning independently. Here, unlike the prevalent paradigm, we show that the TCSs of M. tuberculosis cross-talk extensively, thereby proposing an alternative signalling scenario.


PLoS ONE ◽  
2012 ◽  
Vol 7 (5) ◽  
pp. e37737 ◽  
Author(s):  
Sonja Pawelczyk ◽  
Kathryn A. Scott ◽  
Rebecca Hamer ◽  
Gareth Blades ◽  
Charlotte M. Deane ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document