Structural characterization reveals that a PilZ domain protein undergoes substantial conformational change upon binding to cyclic dimeric guanosine monophosphate

Shin, Jeong Hyun; Ryu, Kyoung‐Seok; Ko, Jong Soo; Lee, Arum; Choi, Byong‐Seok

doi:10.1002/pro.557

Cited by 19 publications

(18 citation statements)

References 20 publications

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“…Several X-ray and nuclear magnetic resonance (NMR) structures of the PilZ domain receptors have now been solved (50,82,83,150,151). These studies have confirmed the bioinformatic (48) and biochemical (52) prediction that two short stretches of residues comprising the PilZ domain consensus, RxxxRx 20 -30 (D/ N)x(S/A)xxG, are involved in c-di-GMP binding ( Fig.…”

Section: Types Of C-di-gmp Receptorsmentioning

confidence: 57%

Cyclic di-GMP: the First 25 Years of a Universal Bacterial Second Messenger

Römling

Galperin

Gomelsky

2013

Microbiol Mol Biol Rev

1,471

1,698

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SUMMARY Twenty-five years have passed since the discovery of cyclic dimeric (3′→5′) GMP (cyclic di-GMP or c-di-GMP). From the relative obscurity of an allosteric activator of a bacterial cellulose synthase, c-di-GMP has emerged as one of the most common and important bacterial second messengers. Cyclic di-GMP has been shown to regulate biofilm formation, motility, virulence, the cell cycle, differentiation, and other processes. Most c-di-GMP-dependent signaling pathways control the ability of bacteria to interact with abiotic surfaces or with other bacterial and eukaryotic cells. Cyclic di-GMP plays key roles in lifestyle changes of many bacteria, including transition from the motile to the sessile state, which aids in the establishment of multicellular biofilm communities, and from the virulent state in acute infections to the less virulent but more resilient state characteristic of chronic infectious diseases. From a practical standpoint, modulating c-di-GMP signaling pathways in bacteria could represent a new way of controlling formation and dispersal of biofilms in medical and industrial settings. Cyclic di-GMP participates in interkingdom signaling. It is recognized by mammalian immune systems as a uniquely bacterial molecule and therefore is considered a promising vaccine adjuvant. The purpose of this review is not to overview the whole body of data in the burgeoning field of c-di-GMP-dependent signaling. Instead, we provide a historic perspective on the development of the field, emphasize common trends, and illustrate them with the best available examples. We also identify unresolved questions and highlight new directions in c-di-GMP research that will give us a deeper understanding of this truly universal bacterial second messenger.

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Section: Types Of C-di-gmp Receptorsmentioning

confidence: 57%

Cyclic di-GMP: the First 25 Years of a Universal Bacterial Second Messenger

Römling

Galperin

Gomelsky

2013

Microbiol Mol Biol Rev

1,471

1,698

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“…PP4397 from Pseudomonas putida binds two molecules of c-di-GMP and undergoes a dimer-to-monomer transition (Ko et al 2010). PA4608 from P. aeruginosa is a single-domain-containing protein that binds to one molecule of c-di-GMP and undergoes rearrangement to expose a negative surface of the protein that is predicted to function in downstream processes (Habazettl et al 2011, Shin et al 2011). These differences in stoichiometry and oligomeric states are predicted to allow for diverse forms of c-di-GMP-dependent regulation (Habazettl et al 2011, Ko et al 2010, Shin et al 2011).…”

Section: C-di-gmp Effector Systemsmentioning

confidence: 99%

Second Messenger Regulation of Biofilm Formation: Breakthroughs in Understanding c-di-GMP Effector Systems

Boyd

O’Toole²

2012

Annu. Rev. Cell Dev. Biol.

206

165

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The second messenger bis-(3′-5′)-cyclic dimeric guanosine monophosphate (c-di-GMP) has emerged as a broadly conserved intracellular signaling molecule. This soluble molecule is important for controlling biofilm formation, adhesion, motility, virulence, and cell morphogenesis in diverse bacterial species. But how is the typical bacterial cell able to coordinate the actions of upward of 50 proteins involved in synthesizing, degrading, and binding c-di-GMP? Understanding the specificity of c-di-GMP signaling in the context of so many enzymes involved in making, breaking, and binding the second messenger will be possible only through mechanistic studies of its output systems. Here we discuss three newly characterized c-di-GMP effector systems that are best understood in terms of molecular and structural detail. As they are conserved across many bacterial species, they likely will serve as central paradigms for c-di-GMP output systems and contribute to our understanding of how bacteria control critical aspects of their biology.

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“…Most members of this family have a conserved motif, RxxxR-D/NxSxxG (1). Conserved residues in this motif are proposed to be critical in interacting with the c-di-GMP ligand, according to the recently published X-ray crystal structures of PlzD and PA4608, two PilZ domain proteins from V. cholerae and P. aeruginosa, respectively (4,21,48).…”

mentioning

confidence: 99%

Evidence for Cyclic Di-GMP-Mediated Signaling in Bacillus subtilis

et al. 2012

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ABSTRACTCyclic di-GMP (c-di-GMP) is a second messenger that regulates diverse cellular processes in bacteria, including motility, biofilm formation, cell-cell signaling, and host colonization. Studies of c-di-GMP signaling have chiefly focused on Gram-negative bacteria. Here, we investigated c-di-GMP signaling in the Gram-positive bacteriumBacillus subtilisby constructing deletion mutations in genes predicted to be involved in the synthesis, breakdown, or response to the second messenger. We found that a putative c-di-GMP-degrading phosphodiesterase, YuxH, and a putative c-di-GMP receptor, YpfA, had strong influences on motility and that these effects depended on sequences similar to canonical EAL and RxxxR—D/NxSxxG motifs, respectively. Evidence indicates that YpfA inhibits motility by interacting with the flagellar motor protein MotA and thatyuxHis under the negative control of the master regulator Spo0A∼P. Based on these findings, we propose that YpfA inhibits motility in response to rising levels of c-di-GMP during entry into stationary phase due to the downregulation ofyuxHby Spo0A∼P. We also present evidence that YpfA has a mild influence on biofilm formation.In toto, our results demonstrate the existence of a functional c-di-GMP signaling system inB. subtilisthat directly inhibits motility and directly or indirectly influences biofilm formation.

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Structural characterization reveals that a PilZ domain protein undergoes substantial conformational change upon binding to cyclic dimeric guanosine monophosphate

Cited by 19 publications

References 20 publications

Cyclic di-GMP: the First 25 Years of a Universal Bacterial Second Messenger

Cyclic di-GMP: the First 25 Years of a Universal Bacterial Second Messenger

Second Messenger Regulation of Biofilm Formation: Breakthroughs in Understanding c-di-GMP Effector Systems

Evidence for Cyclic Di-GMP-Mediated Signaling in Bacillus subtilis

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