{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Heo K"],"funding":["Ministry of Science, ICT and Future Planning","Korea Ministry of Science and ICT","National Research Foundation of Korea"],"pagination":["101626"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8861645"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["298(3)"],"pubmed_abstract":["The bacterial second messenger bis-(3'-5')-cyclic diguanylate monophosphate (c-di-GMP) controls various cellular processes, including motility, toxin production, and biofilm formation. c-di-GMP is enzymatically synthesized by GGDEF domain-containing diguanylate cyclases and degraded by HD-GYP domain-containing phosphodiesterases (PDEs) to 2 GMP or by EAL domain-containing PDE-As to 5'-phosphoguanylyl-(3',5')-guanosine (pGpG). Since excess pGpG feedback inhibits PDE-A activity and thereby can lead to the uncontrolled accumulation of c-di-GMP, a PDE that degrades pGpG to 2 GMP (PDE-B) has been presumed to exist. To date, the only enzyme known to hydrolyze pGpG is oligoribonuclease Orn, which degrades all kinds of oligoribonucleotides. Here, we identified a pGpG-specific PDE, which we named P"],"journal":["The Journal of biological chemistry"],"pubmed_title":["A pGpG-specific phosphodiesterase regulates cyclic di-GMP signaling in Vibrio cholerae."],"pmcid":["PMC8861645"],"funding_grant_id":["NRF-2019R1A2C2004143","NRF-2018R1A5A1025077"],"pubmed_authors":["Kwon S","Seok C","Jang Y","Lee J","Heo K","Lee JW","Ha NC","Seok YJ"],"additional_accession":[]},"is_claimable":false,"name":"A pGpG-specific phosphodiesterase regulates cyclic di-GMP signaling in Vibrio cholerae.","description":"The bacterial second messenger bis-(3'-5')-cyclic diguanylate monophosphate (c-di-GMP) controls various cellular processes, including motility, toxin production, and biofilm formation. c-di-GMP is enzymatically synthesized by GGDEF domain-containing diguanylate cyclases and degraded by HD-GYP domain-containing phosphodiesterases (PDEs) to 2 GMP or by EAL domain-containing PDE-As to 5'-phosphoguanylyl-(3',5')-guanosine (pGpG). Since excess pGpG feedback inhibits PDE-A activity and thereby can lead to the uncontrolled accumulation of c-di-GMP, a PDE that degrades pGpG to 2 GMP (PDE-B) has been presumed to exist. To date, the only enzyme known to hydrolyze pGpG is oligoribonuclease Orn, which degrades all kinds of oligoribonucleotides. Here, we identified a pGpG-specific PDE, which we named P","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Mar","modification":"2025-04-04T20:50:44.133Z","creation":"2025-04-04T20:50:44.133Z"},"accession":"S-EPMC8861645","cross_references":{"pubmed":["35074425"],"doi":["10.1016/j.jbc.2022.101626"]}}