<i>Vibrio cholerae</i>
            VpsT Regulates Matrix Production and Motility by Directly Sensing Cyclic di-GMP

Krasteva, Petya V.; Fong, Jiunn C. N.; Shikuma, Nicholas J.; Beyhan, Sinem; Navarro, M.V.A.S.; Yildiz, Fitnat H.; Sondermann, Holger

doi:10.1126/science.1181185

Cited by 383 publications

(524 citation statements)

References 17 publications

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“…Pel polysaccharide biosynthesis is furthermore regulated in P. aeruginosa by the c-di-GMP receptor protein PelD (91). Recently, a novel c-di-GMP protein that triggers attachment by inducing polysaccharide production was identified in V. cholerae (83). This work demonstrated that the transcriptional regulator VpsT directly senses c-di-GMP to inversely control Vps polysaccharide production and motility.…”

Section: Modulation Of Cyclic Di-gmpmentioning

confidence: 85%

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Sticky Situations: Key Components That Control Bacterial Surface Attachment

Petrova

Sauer

2012

Journal of Bacteriology

319

251

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Section: Modulation Of Cyclic Di-gmpmentioning

confidence: 85%

“…This work demonstrated that the transcriptional regulator VpsT directly senses c-di-GMP to inversely control Vps polysaccharide production and motility. The effect on VpsT, the master regulator for biofilm formation, was found to be due to a change in oligomerization upon c-di-GMP binding rather than phosphorylation (83).…”

Section: Modulation Of Cyclic Di-gmpmentioning

confidence: 99%

Sticky Situations: Key Components That Control Bacterial Surface Attachment

Petrova

Sauer

2012

Journal of Bacteriology

319

251

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“…The affinity of these RNAs for their ligand is very high; class I riboswitches have a K d as tight as 10 pM (23) (1,2,(9)(10)(11)(12)(13)(14)(15)(16). Whereas a few bacteria contain examples of both classes, several species lacking a class I riboswitch use c-di-GMP for signaling and have exclusively a class II riboswitch (19).…”

mentioning

confidence: 99%

“…To alter gene expression or protein activity in response to external or internal signals, c-di-GMP interacts with several proteins (1,2,(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17). In addition, two classes of RNAs have been reported that bind this second messenger, the c-di-GMP-I (class I) and c-di-GMP-II (class II) riboswitches (18,19).…”

mentioning

confidence: 99%

Structural basis of differential ligand recognition by two classes of bis-(3′-5′)-cyclic dimeric guanosine monophosphate-binding riboswitches

Smith

Shanahan

Moore

et al. 2011

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

106

195

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The bis-(3′-5′)-cyclic dimeric guanosine monophosphate (c-di-GMP) signaling pathway regulates biofilm formation, virulence, and other processes in many bacterial species and is critical for their survival. Two classes of c-di-GMP-binding riboswitches have been discovered that bind this second messenger with high affinity and regulate diverse downstream genes, underscoring the importance of RNA receptors in this pathway. We have solved the structure of a c-di-GMP-II riboswitch, which reveals that the ligand is bound as part of a triplex formed with a pseudoknot. The structure also shows that the guanine bases of c-di-GMP are recognized through noncanonical pairings and that the phosphodiester backbone is not contacted by the RNA. Recognition is quite different from that observed in the c-di-GMP-I riboswitch, demonstrating that at least two independent solutions for RNA second messenger binding have evolved. We exploited these differences to design a c-di-GMP analog that selectively binds the c-di-GMP-II aptamer over the c-di-GMP-I RNA. There are several bacterial species that contain both types of riboswitches, and this approach holds promise as an important tool for targeting one riboswitch, and thus one gene, over another in a selective fashion.

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“…An increasing number of proteins responsive to c-di-GMP has been identified (reviewed by Hengge, 2009), including several DNA-binding proteins, i.e. the FleQ regulator in Pseudomonas aeruginosa (Hickman & Harwood, 2008), the VpsT protein in Vibrio cholerae (Krasteva et al, 2010) and the CLP protein in Xanthomonas campestris (Chin et al, 2010). In addition, c-di-GMP can regulate gene expression through direct binding to riboswitch elements in mRNAs (Sudarsan et al, 2008), bypassing the need for c-di-GMPbinding regulatory proteins.…”

Section: Introductionmentioning

confidence: 99%

The diguanylate cyclase YddV controls production of the exopolysaccharide poly-N-acetylglucosamine (PNAG) through regulation of the PNAG biosynthetic pgaABCD operon

et al. 2010

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In Gram-negative bacteria, production of adhesion factors and extracellular polysaccharides (EPS) is promoted by the activity of diguanylate cyclases (DGCs), a class of enzymes able to catalyse the synthesis of the signal molecule bis-(39,59)-cyclic di-guanylic acid (c-di-GMP). In this report we show that in Escherichia coli, overexpression of the YddV protein, but not of other DGCs such as AdrA and YcdT, induces the production of the EPS poly-N-acetylglucosamine (PNAG) by stimulating expression of pgaABCD, the PNAG-biosynthetic operon. Stimulation of PNAG production and activation of pgaABCD expression by the YddV protein are abolished by inactivation of its GGDEF motif, responsible for DGC activity. Consistent with the effects of YddV overexpression, inactivation of the yddV gene negatively affects pgaABCD transcription and PNAG-mediated biofilm formation. pgaABCD regulation by the yddV gene also takes place in a mutant carrying a partial deletion of the csrA gene, which encodes the main regulator of pgaABCD expression, suggesting that YddV does not regulate pgaABCD through modulation of CsrA activity. Our results demonstrate that PNAG production does not simply respond to intracellular c-di-GMP concentration, but specifically requires the DGC activity of the YddV protein, thus supporting the notion that in E. coli, c-di-GMP biosynthesis by a given DGC protein triggers regulatory events that lead to activation of specific sets of EPS biosynthetic genes or proteins. INTRODUCTIONMost bacteria are able to switch between two different 'lifestyles': single cells (planktonic mode) and biofilm, i.e. a sessile microbial community. Biofilm and planktonic cells differ significantly in their physiology, in their gene expression pattern and even in their morphology. In particular, biofilm cells are characterized by production of adhesion factors and extracellular polysaccharides (EPS), resistance to environmental stresses, and lower sensitivity to antibiotics compared with planktonic cells (Costerton et al., 1995;Anderl et al., 2000;Harrison et al., 2007Harrison et al., , 2009).Transition from planktonic cells to biofilm is regulated by environmental and physiological cues, relayed to the bacterial cell by signal molecules or 'second messengers'. A second messenger, bis-(39,59)-cyclic diguanylic acid, better known as cyclic-di-GMP (c-di-GMP), plays a pivotal role in biofilm formation and maintenance by stimulating production of EPS and adhesion factors (Ross et al., 1991;Simm et al., 2004;Kader et al., 2006;Weber et al., 2006). In addition, c-di-GMP biosynthesis affects important cellular processes, such as morphological differentiation and cell replication in Caulobacter crescentus (Paul et al., 2004), cell motility (Méndez-Ortiz et al., 2006; Jonas et al., 2008) and virulence factor production (Kulasakara et al., 2006;Hammer & Bassler, 2009). In Enterobacteria, c-di-GMP seems to be involved in regulation of adhesion factors, such as curli and cellulose, important for adaptation and survival outside the warm-blooded hos...

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Vibrio cholerae VpsT Regulates Matrix Production and Motility by Directly Sensing Cyclic di-GMP

Cited by 383 publications

References 17 publications

Sticky Situations: Key Components That Control Bacterial Surface Attachment

Sticky Situations: Key Components That Control Bacterial Surface Attachment

Structural basis of differential ligand recognition by two classes of bis-(3′-5′)-cyclic dimeric guanosine monophosphate-binding riboswitches

The diguanylate cyclase YddV controls production of the exopolysaccharide poly-N-acetylglucosamine (PNAG) through regulation of the PNAG biosynthetic pgaABCD operon

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