Cell-cell signaling in Xanthomonas campestris involves an HD-GYP domain protein that functions in cyclic di-GMP turnover. [PDF]
Proc Natl Acad Sci U S A, 2006 HD-GYP is a protein domain of unknown biochemical function implicated in bacterial signaling and regulation. In the plant pathogen Xanthomonas campestris pv.
Ryan RP +10 more
europepmc +5 more sources
Biochemistry, 2020 The second messenger bis(3′,5′)-cyclic dimeric guanosine monophosphate (c-di-GMP) regulates numerous important physiological functions in bacteria.
Ariki Matsuoka (2028430) +7 more
core +3 more sources
<i>Vibrio cholerae</i> V-cGAP3 Is an HD-GYP Phosphodiesterase with a Metal Tunable Substrate Selectivity. [PDF]
Biochemistry, 2022 Cyclic dinucleotides (CDNs) are signaling molecules involved in the immune response and virulence factor production. CDN cellular levels are fine-tuned by metal-dependent phosphodiesterases (PDEs), among which HD-GYPs make up a subclass of the larger HD-domain protein superfamily.
Sun S, Wang R, Pandelia ME.
europepmc +3 more sources
Second messengers and divergent HD-GYP phosphodiesterases regulate 3',3'-cGAMP signaling. [PDF]
Mol Microbiol, 2020 Summary 3′,3′‐cyclic GMP‐AMP (cGAMP) is the third cyclic dinucleotide (CDN) to be discovered in bacteria. No activators of cGAMP signaling have yet been identified, and the signaling pathways for cGAMP have been inferred to display a narrow distribution based upon the characterized synthases, DncV and Hypr GGDEFs.
Wright TA +7 more
europepmc +6 more sources
HD-[HD-GYP] Phosphodiesterases: Activities and Evolutionary Diversification within the HD-GYP Family. [PDF]
Biochemistry, 2020 Cyclic dinucleotides are signaling molecules that modulate many processes, including immune response and virulence factor production. Their cellular levels in bacteria are fine-tuned by metal-dependent phosphodiesterases, namely, the EAL and HD-GYP proteins, with HD-GYPs belonging to the larger HD domain superfamily.
Sun S, Pandelia ME.
europepmc +4 more sources
Sequence Conservation, Domain Architectures, and Phylogenetic Distribution of the HD-GYP Type c-di-GMP Phosphodiesterases. [PDF]
J Bacteriol, 2022 ABSTRACT The HD-GYP domain, named after two of its conserved sequence motifs, was first described in 1999 as a specialized version of the widespread HD phosphohydrolase domain that had additional highly conserved amino acid residues.
Galperin MY, Chou SH.
europepmc +4 more sources
Archaeal Genes Code for GGDEF Domain Proteins With Diguanylate Cyclase Activity. [PDF]
Mol MicrobiolA biofilm‐like mode of growth is hypothesized to be required for the emergence of cellular life. Occurrence of common biofilm gene products in current Bacteria and Archaea is an indication for their previous presence in the last universal common ancestor LUCA and perhaps even in the first universal common ancestor FUCA.
Sidorov R +6 more
europepmc +2 more sources
Active Site Metal Occupancy and Cyclic Di-GMP Phosphodiesterase Activity of Thermotoga maritima HD-GYP. [PDF]
Biochemistry, 2016 HD-GYPs make up a subclass of the metal-dependent HD phosphohydrolase superfamily and catalyze conversion of cyclic di(3',5')-guanosine monophosphate (c-di-GMP) to 5'-phosphoguanylyl-(3'→5')-guanosine (pGpG) and GMP. Until now, the only reported crystal structure of an HD-GYP that also exhibits c-di-GMP phosphodiesterase activity contains a His ...
Miner KD, Kurtz DM.
europepmc +4 more sources
An HD-GYP cyclic di-guanosine monophosphate phosphodiesterase with a non-heme diiron-carboxylate active site. [PDF]
Biochemistry, 2013 The intracellular level of the ubiquitous bacterial secondary messenger, cyclic di-(3',5')-guanosine monophosphate (c-di-GMP), represents a balance between its biosynthesis and degradation, the latter via specific phosphodiesterases (PDEs). One class of c-di-GMP PDEs contains a characteristic HD-GYP domain. Here we report that an HD-GYP PDE from Vibrio
Miner KD, Klose KE, Kurtz DM.
europepmc +4 more sources
BMC Genomics, 2022 Background Bis-(3′-5′)-cyclic dimeric guanosine monophosphate (c-di-GMP) is a bacterial second messenger that affects diverse processes in different bacteria, including the cell cycle, motility, and biofilm formation.
Sonja Koppenhöfer, Andrew S. Lang
doaj +1 more source