Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Cell-cell signaling in Xanthomonas campestris involves an HD-GYP domain protein that functions in cyclic di-GMP turnover.

Proceedings of the National Academy of Sciences of the United States of America - 25 Apr 2006

Ryan Robert P, Fouhy Yvonne, Lucey Jean F, Crossman Lisa C, Spiro Stephen, He Ya-Wen, Zhang Lian-Hui, Heeb Stephan, Cámara Miguel, Williams Paul, Dow J Maxwell

Abstract excerpt

HD-GYP is a protein domain of unknown biochemical function implicated in bacterial signaling and regulation. In the plant pathogen Xanthomonas campestris pv. campestris, the synthesis of virulence factors and dispersal of biofilms are positively controlled by a two-component signal transduction system comprising the HD-GYP domain regulatory protein RpfG and cognate sensor RpfC and by cell-cell signaling mediated...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cyclic GMP
Share to DNA, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genes, Bacterial

Share to Mutagenesis, Site-Directed

Share to Pseudomonas aeruginosa

Share to Recombinant Proteins

Share to Virulence

Share to Xanthomonas campestris

Source

Open in PubMed Open full text

Identifiers

PMID: 16611728
DOI: 10.1073/pnas.0600345103
PMCID: PMC1458946

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cell-cell signaling in Xanthomonas campestris involves an HD-GYP domain protein that functions in cyclic di-GMP turnover.PMID 16611728Read ↗

Proteomics analysis of the regulatory role of Rpf/DSF cell-to-cell signaling system in the virulence of Xanthomonas campestris.Semantic proximity Read ↗

pGpG-signaling regulates virulence and global transcriptomic targets in <i>Erwinia amylovora</i>Semantic proximity Read ↗

Cyclic-di-GMP-mediated signalling within the sigma network of Escherichia coli.Semantic proximity Read ↗

A two-component system involving an HD-GYP domain protein links cell-cell signalling to pathogenicity gene expression in Xanthomonas campestris.Semantic proximity Read ↗

Phenotypic-genotypic analysis of GGDEF/EAL/HD-GYP domain-encoding genes in Pseudomonas putida.Semantic proximity Read ↗

Comprehensive overexpression analysis of cyclic-di-GMP signalling proteins in the phytopathogen Pectobacterium atrosepticum reveals diverse effects on motility and virulence phenotypes.Semantic proximity Read ↗

Genetic analysis of two phosphodiesterases reveals cyclic diguanylate regulation of virulence factors in Dickeya dadantii.Semantic proximity Read ↗

Phenotypic Analysis of GGDEF/EAL Domain Protein Functions in Phytopathogenic <i>Pantoea ananatis</i>Semantic proximity Read ↗

Crystal structure of an HD-GYP domain cyclic-di-GMP phosphodiesterase reveals an enzyme with a novel trinuclear catalytic iron centre.Semantic proximity Read ↗

Novel cyclic di-GMP effectors of the YajQ protein family control bacterial virulence.Semantic proximity Read ↗

A systematic analysis of the in vitro and in vivo functions of the HD-GYP domain proteins of Vibrio cholerae.Semantic proximity Read ↗

Regulation of the synthesis of cyclic glucan in Xanthomonas campestris by a diffusible signal molecule.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.