A photosensory two-component system regulates bacterial cell attachment

Purcell, Erin B.; Siegal-Gaskins, Dan; Rawling, David; Fiebig, Aretha; Crosson, Sean

doi:10.1073/pnas.0705887104

Cited by 166 publications

(205 citation statements)

References 27 publications

Supporting

Mentioning

197

Contrasting

Unclassified

Order By: Relevance

“…In C. crescentus, based on genetic experiments, the SDRR LovR has been proposed to regulate PhyR activity negatively by functioning as a phosphate sink, together with its cognate kinase LovK (21). In addition, LovK controls cell adhesion by an unknown mechanism (38), but independent of the σ EcfG ortholog, SigT (39). Although the physiological relevance was not explored, these data suggest that both functions might coexist.…”

Section: Discussionmentioning

confidence: 98%

See 1 more Smart Citation

Complex two-component signaling regulates the general stress response in Alphaproteobacteria

Kaczmarczyk¹,

Hochstrasser²,

Vorholt³

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

117

View full text Add to dashboard Cite

Significance Bacteria possess many regulatory systems to monitor their environment and adapt their physiology accordingly. Whereas most systems sense one specific signal, the general stress response (GSR) is activated by many signals and protects cells against a wide range of adverse conditions. In Alphaproteobacteria, the GSR is controlled by the response regulator PhyR, but little is known about the upstream pathways. Here, we establish the GSR as a complex regulatory network composed of a particular family of partially redundant sensor kinases and of additional response regulators that modulate PhyR activity in Sphingomonas melonis . Given the broad conservation of this kinase family, it is possible that it plays a general role in the GSR in Alphaproteobacteria.

show abstract

Section: Discussionmentioning

confidence: 98%

“…2G). Finally, as discussed above, LovK of C. crescentus is proposed to serve a dual role in GSR regulation and cell adhesion (21,38,39). Thus, it might be possible that other HRXXN kinases function with PhyR and a second response regulator in branched pathways.…”

Section: Discussionmentioning

confidence: 99%

Complex two-component signaling regulates the general stress response in Alphaproteobacteria

Kaczmarczyk¹,

Hochstrasser²,

Vorholt³

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

117

View full text Add to dashboard Cite

show abstract

“…LOV domaincontaining proteins are distributed not only in plants but also in many other organisms. For example, WC-1 and VVD are found in the ascomycete fungus Neurospora crassa (8), aureochrome in the alga Vaucheria frigida (9), and bacterial histidine kinases in the animal pathogenic bacterium Brucella abortus (10) and in the stalked bacterium Caulobacter crescentus (11). These proteins have all been shown to function as photoreceptors.…”

mentioning

confidence: 99%

FMN Binding and Photochemical Properties of Plant Putative Photoreceptors Containing Two LOV Domains, LOV/LOV Proteins

Kasahara

Torii

Fujita

et al. 2010

Journal of Biological Chemistry

View full text Add to dashboard Cite

Four photoreceptor families have been found from plants including phytochrome, cryptochrome, phototropin, and ADO/ FKF/LKP/ZTL family proteins. Among them, phototropin and ADO/FKF/LKP/ZTL use a common light-sensing domain, LOV domain (1). The LOV domain was found as the lightsensing domain of the phototropin (PHOT1 and PHOT2) (2-4) and has been well characterized (1, 5-7). LOV domaincontaining proteins are distributed not only in plants but also in many other organisms. For example, WC-1 and VVD are found in the ascomycete fungus Neurospora crassa (8), aureochrome in the alga Vaucheria frigida (9), and bacterial histidine kinases in the animal pathogenic bacterium Brucella abortus (10) and in the stalked bacterium Caulobacter crescentus (11). These proteins have all been shown to function as photoreceptors.Six genes encoding LOV domain-containing proteins are found in the genome of Arabidopsis thaliana. Among them, two encode phototropins, and three encode the ADO/FKF/ LKP/ZTL family proteins, proteins involved in circadian clock and photoperiod-dependent flowering functions (12-15). All of the LOV domains of phototropins and ADO/FKF/LKP/ZTL family proteins are shown to bind FMN (2,4,15,16). In addition to those above, there exists a unique LOV domain-containing protein, referred to as PAS/LOV protein (PLP), 2 which contains a PAS domain followed by a LOV domain (1, 17).Ogura et al. (18) screened for proteins interacting with A. thaliana PLP using the yeast two-hybrid system. They isolated VTC2 (vitamin C defective 2), VTC2L (VTC2-like), and BLH10A and BLH10B (BEL1-like homeodomain 10 A and B proteins) as interacting proteins in yeast cells. The molecular interactions between PLP and VTC2L, BLH10A, or BLH10B in yeast were dependent on blue light irradiation, suggesting that PLP may function as a photoreceptor (18). Blue light treatment diminished the interaction. However, the flavin binding and photochemical properties of the A. thaliana PLP are unclear because the recombinant protein expressed in Escherichia coli did not show absorption spectra of flavin-binding proteins (18).In this study, we isolate cDNAs coding for PLP homologs from tomato (Solanum lycopersicum) and the moss Physcomitrella patens, and phylogenetic analysis shows that the PAS domains of the homologs, even the PAS domain of A. thaliana PLP, are closely related to the LOV domain. Thus, we propose that the isolated LOV domain-containing protein should be referred to as LOV/LOV protein (LLP), instead of PLP. Here, we analyze chromophore binding and photochemical properties of LLP from S. lycopersicum using wild-type and mutant proteins expressed in E. coli. We also examine both LOV domains of both PpLLPs for FMN binding and photochemical properties.

show abstract

“…The sensor histidine kinase LovK binds a flavin mononucleotide (FMN) cofactor (33) via an N-terminal LOV (light, oxygen, and voltage) domain (16) and has the capacity to perceive both blue light and changes in the reductive state of its environment (33,34). LovK and LovR are encoded from a single locus on the C. crescentus chromosome (Fig.…”

mentioning

confidence: 99%

The LovK-LovR Two-Component System Is a Regulator of the General Stress Pathway in Caulobacter crescentus

2012

Self Cite

View full text Add to dashboard Cite

A conserved set of regulators control the general stress response in Caulobacter crescentus , including σ T , its anti-σ factor NepR, the anti-anti-σ factor PhyR, and the transmembrane sensor kinase PhyK. We report that the soluble histidine kinase LovK and the single-domain response regulator LovR also function within the C. crescentus general stress pathway. Our genetic data support a model in which LovK-LovR functions upstream of σ T by controlling the phosphorylation state and thus anti-anti-σ activity of PhyR. Transcription of lovK and lovR is independently activated by stress through a mechanism that requires sigT and phyR . Conversely, lovK and lovR function together to repress transcription of the general stress regulon. Concordant with a functional role of the LovK-LovR two-component system as a negative regulator of the general stress pathway, lovK - lovR -null mutants exhibit increased cell survival after osmotic stress, while coordinate overexpression of lovK and lovR attenuates cell survival relative to that of the wild type. Notably, lovK can complement the transcriptional and cell survival defects of a phyK -null mutant when lovR is deleted. Moreover, in this same genetic background, σ T -dependent transcription is activated in response to osmotic stress. This result suggests that flavin-binding LOV (light, oxygen, or voltage) histidine kinases are competent to perceive cytoplasmic signals in addition to the environmental signal blue light. We conclude that the PhyK-PhyR and LovK-LovR two-component signaling systems coordinately regulate stress physiology in C. crescentus .

show abstract

A photosensory two-component system regulates bacterial cell attachment

Cited by 166 publications

References 27 publications

Complex two-component signaling regulates the general stress response in Alphaproteobacteria

Complex two-component signaling regulates the general stress response in Alphaproteobacteria

FMN Binding and Photochemical Properties of Plant Putative Photoreceptors Containing Two LOV Domains, LOV/LOV Proteins

The LovK-LovR Two-Component System Is a Regulator of the General Stress Pathway in Caulobacter crescentus

Contact Info

Product

Resources

About