Role of the GGDEF regulator PleD in polar development of <i>Caulobacter crescentus</i>

Aldridge, Phillip D.; Paul, Ralf; Goymer, Patrick; Rainey, Paul B.; Jenal, Urs

doi:10.1046/j.1365-2958.2003.03401.x

Cited by 262 publications

(261 citation statements)

References 56 publications

(124 reference statements)

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“…Given the sequence homology (74 % identity) between P. fluorescens SBW25 and P. aeruginosa PAO1 WspR (recently shown to function as a DGC by Hickman et al, 2005) and the fact that WspR R129C complements PleD activity in C. crescentus (Aldridge et al, 2003), it was reasonable to assume that WspR is a DGC, catalysing the formation of c-di-GMP from two molecules of GTP. Nevertheless, it was important to independently verify DGC activity for SBW25 WspR.…”

Section: Resultsmentioning

confidence: 99%

“…Cloning was carried out in accordance with standard molecular biology techniques (Sambrook et al, 1989). pME6010-wspR was constructed by ligation of wspR, excised as a BamHI/EcoRI fragment from pWspR12 (Aldridge et al, 2003) between the BglII and EcoRI sites of pME6010 (Heeb et al, 2000), destroying the BglII site in the process. pET42b-wspR was constructed by ligation of the relevant wspR PCR fragment (amplified with primers WspRPurFor and WspRPurRev from pME6010-wspR), between the XhoI and NdeI sites of pET42b (Novagen).…”

Section: Methodsmentioning

confidence: 99%

“…For example, PleD controls the onset of motility during the C. crescentus cell cycle (Aldridge et al, 2003;Paul et al, 2004). In Pseudomonas aeruginosa, autoaggregation is controlled by the GGDEF response regulator WspR (D'Argenio et al, 2002;Hickman et al, 2005), and twitching motility by FimX, which contains GGDEF and EAL domains (Huang et al, 2003;Kazmierczak et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

“…A wspR : : mini-Tn5 WS mutant displays a smooth colony morphology (Spiers et al, 2002), and does not produce cellulose or attach to surfaces (Spiers et al, 2003). Expression of wspR in trans stimulates attachment and exopolysaccharide synthesis in various species (D'Argenio et al, 2002;Aldridge et al, 2003;Goymer et al, 2006;Ude et al, 2006). The evolutionary cause of LSWS is a single point mutation in the gene encoding the WspF methylesterase, which results in overactivation of the WspE kinase and constitutive activation of the primary output component of the Wsp pathway, WspR (Bantinaki et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

“…In addition, constitutively active [e.g. WspR 19 (R129C); D' Argenio et al, 2002;Aldridge et al, 2003] and dominant-negative [e.g. WspR 9 (G296R)] wspR alleles have been identified.…”

Section: Introductionmentioning

confidence: 99%

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The structure–function relationship of WspR, a Pseudomonas fluorescens response regulator with a GGDEF output domain

et al. 2007

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The GGDEF response regulator WspR couples the chemosensory Wsp pathway to the overproduction of acetylated cellulose and cell attachment in the Pseudomonas fluorescens SBW25 wrinkly spreader (WS) genotype. Here, it is shown that WspR is a diguanylate cyclase (DGC), and that DGC activity is elevated in the WS genotype compared to that in the ancestral smooth (SM) genotype. A structure-function analysis of 120 wspR mutant alleles was employed to gain insight into the regulation and activity of WspR. Firstly, 44 random and defined pentapeptide insertions were produced in WspR, and the effects determined using assays based on colony morphology, attachment to surfaces and cellulose production. The effects of mutations within WspR were interpreted using a homology model, based on the crystal structure of Caulobacter crescentus PleD. Mutational analyses indicated that WspR activation occurs as a result of disruption of the interdomain interface, leading to the release of effector-domain repression by the N-terminal receiver domain. Quantification of attachment and cellulose production raised significant questions concerning the mechanisms of WspR function. The conserved RYGGEEF motif of WspR was also subjected to mutational analysis, and 76 single amino acid residue substitutions were tested for their effects on WspR function. The RYGGEEF motif of WspR is functionally conserved, with almost every mutation abolishing function.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…In addition, constitutively active [e.g. WspR 19 (R129C); D' Argenio et al, 2002;Aldridge et al, 2003] and dominant-negative [e.g. WspR 9 (G296R)] wspR alleles have been identified.…”

Section: Introductionmentioning

confidence: 99%

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The structure–function relationship of WspR, a Pseudomonas fluorescens response regulator with a GGDEF output domain

et al. 2007

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Initial steps of the pathogenesis of the infection caused byStreptococcus suis: fighting against nonspecific defenses

et al. 2016

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Edited by Wilhelm JustInteractions between a bacterial pathogen and its potentially susceptible host are initiated with the colonization step. During respiratory/oral infection, the pathogens must compete with the normal microflora, resist defense mechanisms of the local mucosal immunity, and finally reach, adhere, and breach the mucosal epithelial cell barrier in order to induce invasive disease. This is the case during infection by the swine and zoonotic pathogen Streptococcus suis, which is able to counteract mucosal barriers to induce severe meningitis and sepsis in swine and in humans. The initial steps of the pathogenesis of S. suis infection has been a neglected area of research, overshadowed by studies on the systemic and central nervous phases of the disease. In this Review article, we provide for the first time, an exclusive focus on S. suis colonization and the potential mechanisms involved in S. suis establishment at the mucosa, as well as the mechanisms regulating mucosal barrier breakdown. The role of mucosal immunity is also addressed. Finally, we demystify the extensive list of putative adhesins and virulence factors reported to be involved in the initial steps of pathogenesis by S. suis.

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Regulatory Systems: Two‐Component

Raivio

2019

Encyclopedia of Life Sciences

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Two‐component signal transduction (TCST) systems constitute a large class of regulatory proteins that function as signal transducers. Each system comprises a sensor or histidine kinase (HK) and an effector or response regulator (RR), which communicate through a conserved set of phosphotransfer reactions to effect adaptive changes in response to specific environmental signals. HKs and RRs are modular in nature, with variable sensory and output structures appended to the conserved domains that facilitate phosphotransfer mediated signal transduction. Input signals trigger successive conformational changes in domains and protein:protein interactions that alter phosphotransfer, and ultimately an output response mediated by the phosphorylated RR. TCST systems are abundant in bacteria and many microbes utilise multiple TCST pathways to sense and respond to a plethora of environmental and physiological changes. Specificity between cognate HKs and RRs is largely maintained through co‐evolving residues at a conserved interface where the RR docks on the HK. TCST systems are integrated into cellular signalling networks and interact with macromolecules and proteins that connect them to salient regulatory pathways and cellular functions. The current state of knowledge around TCST systems will be summarised, emphasising findings published since the first version of this article in 2006. Key Concepts A prototypical two‐component system is made up of a membrane‐bound sensory histidine kinase that senses a unique environmental or cellular parameter and a cytoplasmic response regulator that controls an adaptive response. HKs and RRs communicate through phosphotransfer reactions that are mediated by conserved domains; signal sensing alters the ratio of HK kinase to phosphatase activity to change the function of the RR by altering its phosphorylation status. HKs and RRs are organised in a modular fashion; a variety of sensing domains can be appended to the HK enzymatic module while diverse output domains with DNA binding, RNA binding, enzymatic activity or protein binding functions are often fused to the C‐terminal end of the response regulator phosphorylated receiver (REC) domain. The HK is a dimer containing a catalytic domain composed of two DHp and CA domains. The DHp domain consists of a d imer of two alpha helices connected by a flexible linker that makes a four‐helical bundle and contains the conserved h istidine that is the site of auto p hosphorylation. The CA domain resembles other ATP‐binding folds and is the enzymatic portion of the HK. The RR consists at its N‐terminus of the conserved receiver (REC) domain, which consists of a five‐stranded beta sheet surrounded by alpha helices and contains the conserved aspartate that is the site of phosphorylation. Signals are detected through conformational changes in a sensory domain that are propagated through some combination of rotational, piston and order to disorder transitions by alpha‐helical transduction elements to the cytoplasmic enzymatic domain of the HK. These movements lead to alterations in HK dimer symmetry that dictate kinase or phosphatase activity. In the inactive state, the cytoplasmic DHp and CA domains of the HK are organised in a symmetrical fashion with the CA domain juxtaposed against the membrane‐proximal end of the DHp four‐helical bundle. The RR REC domain can interact with the inactive HK DHp four‐helical bundle at a more membrane‐distal location in an orientation that would facilitate dephosphorylation of the aspartate. The active, kinase state of the HK is asymmetrical due to a bend or kink in the DHp domain that leads to one CA domain adopting a looser association that positions it well for phosphorylation of a histidine residue. A single RR REC domain can bind near the other CA domain, which is more closely associated with the DHp domain, in a conformation supporting phosphorylation of the aspartate residue utilising the phosphorylated histidine as a substrate. Repeated cycles of DHp domain bending and RR REC domain binding are hypothesised to support successive rounds of HK autophosphorylation and RR phosphorylation in response to signal inputs received from the sensory domain. HKs and RRs regulate and interact with other macromolecules and proteins to connect signalling pathways, coordinate their activities and sense environmental parameters and changes to cellular physiology.

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Role of the GGDEF regulator PleD in polar development of Caulobacter crescentus

Cited by 262 publications

References 56 publications

The structure–function relationship of WspR, a Pseudomonas fluorescens response regulator with a GGDEF output domain

The structure–function relationship of WspR, a Pseudomonas fluorescens response regulator with a GGDEF output domain

Initial steps of the pathogenesis of the infection caused byStreptococcus suis: fighting against nonspecific defenses

Regulatory Systems: Two‐Component

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