NMR structure and binding studies confirm that PA4608 from <i>Pseudomonas aeruginosa</i> is a PilZ domain and a c‐di‐GMP binding protein

Ramelot, Theresa; Yee, Adelinda; Cort, John; Semesi, A.; Arrowsmith, C.H.; Kennedy, Michael A.

doi:10.1002/prot.21199

Cited by 78 publications

(83 citation statements)

References 33 publications

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“…Binding of c-di-GMP by PilZ Proteins-To date, only three PilZ domain proteins have been shown to bind c-di-GMP, including cellulose synthase from G. xylinus, YcgR from E. coli, and PA4608 from P. aeruginosa (3,39,40). Here we show that two V. cholerae PilZ proteins (PlzC and PlzD) present in cell extracts, as well as purified, bind c-di-GMP specifically and with submicromolar affinities.…”

Section: Discussionmentioning

confidence: 68%

“…Evidence in support of this claim is as follows. 1) Three proteins known to bind c-di-GMP contain a PilZ domain, including cellulose synthase from G. xylinus, YcgR from E. coli, and PA4608 from P. aeruginosa (3,37,38,39,40). 2) Several PilZ-containing proteins have been characterized by mutational analysis and appear to regulate phenotypes associated with c-di-GMP-mediated signaling pathways.…”

Section: Bis(3ј5ј)-cyclic Diguanylic Acid (C-di-gmp)mentioning

confidence: 99%

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PilZ Domain Proteins Bind Cyclic Diguanylate and Regulate Diverse Processes in Vibrio cholerae

Pratt

Tamayo

Tischler³

et al. 2007

Journal of Biological Chemistry

180

205

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Cyclic diguanylate (c-di-GMP) is an allosteric activator and second messenger implicated in the regulation of a variety of biological processes in diverse bacteria. In Vibrio cholerae, c-di-GMP has been shown to inversely regulate biofilm-specific and virulence gene expression, suggesting that c-di-GMP signaling is important for the transition of V. cholerae from the environment to the host. However, the mechanism behind this regulation remains unknown. Recently, it was proposed that the PilZ protein domain represents a c-di-GMP-binding domain. Here we show that V. cholerae PilZ proteins bind c-di-GMP specifically and are involved in the regulation of biofilm formation, motility, and virulence. These findings confirm a role for PilZ proteins as c-di-GMP-sensing proteins within the c-di-GMP signaling network.

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Section: Discussionmentioning

confidence: 68%

Section: Bis(3ј5ј)-cyclic Diguanylic Acid (C-di-gmp)mentioning

confidence: 99%

PilZ Domain Proteins Bind Cyclic Diguanylate and Regulate Diverse Processes in Vibrio cholerae

Pratt

Tamayo

Tischler³

et al. 2007

Journal of Biological Chemistry

180

205

View full text Add to dashboard Cite

show abstract

“…A search for similar structures in the PDB by using VAST (19) yielded many significant hits. Several of the similar structures were members of the PilZ domain, which binds bis-(3Ј-5Ј)-cyclic dimeric guanosine monophosphate (c-di-GMP) and is involved in bacterial signaling (20). Some other similar structures were members of the pyridoxamine 5Ј-phosphate oxidase families (21).…”

Section: Structural Similarity Between Gpvn and A Tail Tube Protein Fmentioning

confidence: 99%

The phage λ major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system

Pell

Kanelis

Donaldson

et al. 2009

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

258

276

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Most bacteriophages possess long tails, which serve as the conduit for genome delivery. We report the solution structure of the N-terminal domain of gpV, the protein comprising the major portion of the noncontractile phage tail tube. This structure is very similar to a previously solved tail tube protein from a contractile-tailed phage, providing the first direct evidence of an evolutionary connection between these 2 distinct types of phage tails. A remarkable structural similarity is also seen to Hcp1, a component of the bacterial type VI secretion system. The hexameric structure of Hcp1 and its ability to form long tubes are strikingly reminiscent of gpV when it is polymerized into a tail tube. These data coupled with other similarities between phage and type VI secretion proteins support an evolutionary relationship between these systems. Using Hcp1 as a model, we propose a polymerization mechanism for gpV involving several disorder-toorder transitions.NMR structure ͉ disordered regions ͉ macromolecular assembly

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“…Several binding devices for c-di-GMP, apart from c-di-GMP metabolic enzymes, have been identified recently. These binding devices are the proteins that contain the PilZ domain (16)(17)(18)(19)(20)(21)(22), the PelD protein (23), which contains the RxxD motif, the c-di-GMPresponsive transcriptional regulator FleQ (24), and a first class of widely distributed riboswitches (25).…”

mentioning

confidence: 99%

Genetic reductionist approach for dissecting individual roles of GGDEF proteins within the c-di-GMP signaling network in Salmonella

Solano

García

Latasa

et al. 2009

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

116

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Bacteria have developed an exclusive signal transduction system involving multiple diguanylate cyclase and phosphodiesterase domain-containing proteins (GGDEF and EAL/HD-GYP, respectively) that modulate the levels of the same diffusible molecule, 3 -5 -cyclic diguanylic acid (c-di-GMP), to transmit signals and obtain specific cellular responses. Current knowledge about c-di-GMP signaling has been inferred mainly from the analysis of recombinant bacteria that either lack or overproduce individual members of the pathway, without addressing potential compensatory effects or interferences between them. Here, we dissected c-di-GMP signaling by constructing a Salmonella strain lacking all GGDEF-domain proteins and then producing derivatives, each restoring 1 protein. Our analysis showed that most GGDEF proteins are constitutively expressed and that their expression levels are not interdependent. Complete deletion of genes encoding GGDEFdomain proteins abrogated virulence, motility, long-term survival, and cellulose and fimbriae synthesis. Separate restoration revealed that 4 proteins from Salmonella and 1 from Yersinia pestis exclusively restored cellulose synthesis in a c-di-GMP-dependent manner, indicating that c-di-GMP produced by different GGDEF proteins can activate the same target. However, the restored strain containing the STM4551-encoding gene recovered all other phenotypes by means of gene expression modulation independently of c-di-GMP. Specifically, fimbriae synthesis and virulence were recovered through regulation of csgD and the plasmid-encoded spvAB mRNA levels, respectively. This study provides evidence that the regulation of the GGDEF-domain proteins network occurs at 2 levels: a level that strictly requires c-di-GMP to control enzymatic activities directly, restricted to cellulose synthesis in our experimental conditions, and another that involves gene regulation for which c-di-GMP synthesis can be dispensable.biofilm formation ͉ Salmonella virulence ͉ signal transduction system cellulose ͉ STM4551

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NMR structure and binding studies confirm that PA4608 from Pseudomonas aeruginosa is a PilZ domain and a c‐di‐GMP binding protein

Cited by 78 publications

References 33 publications

PilZ Domain Proteins Bind Cyclic Diguanylate and Regulate Diverse Processes in Vibrio cholerae

PilZ Domain Proteins Bind Cyclic Diguanylate and Regulate Diverse Processes in Vibrio cholerae

The phage λ major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system

Genetic reductionist approach for dissecting individual roles of GGDEF proteins within the c-di-GMP signaling network in Salmonella

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