Progress in understanding of the molecular basis underlying functional diversification of cyclic di-nucleotide turnover proteins

dc.check.date2017-05-28
dc.check.infoAccess to this article is restricted until 6 months after publication by the request of the publisher.en
dc.contributor.authorRömling, Ute
dc.contributor.authorLiang, Zhao-Xun
dc.contributor.authorDow, J. Maxwell
dc.contributor.funderSvenska Forskningsrådet Formasen
dc.contributor.funderWellcome Trusten
dc.contributor.funderScience Foundation Irelanden
dc.contributor.funderMinistry of Education - Singaporeen
dc.date.accessioned2017-01-10T14:48:46Z
dc.date.available2017-01-10T14:48:46Z
dc.date.issued2016-12-18
dc.date.updated2017-01-10T14:30:23Z
dc.description.abstractCyclic di-GMP was the first cyclic di-nucleotide second messenger described, presaging the discovery of additional cyclic di-nucleotide messengers in bacteria and eukaryotes. The GGDEF diguanylate cyclase (DGC) and EAL and HD-GYP phosphodiesterase (PDE) domains conduct the turnover of cyclic di-GMP. These three unrelated domains belong to superfamilies that exhibit significant variations in function, to include both enzymatically active and inactive members with a subset involved in synthesis and degradation of other cyclic di-nucleotides. Here we summarize current knowledge of sequence and structural varitions that underpin the functional diversification of cyclic di-GMP turnover proteins. Moreover, we highlight that superfamily diversification is not restricted to cyclic di-GMP signaling domains, as particular DHH/DHHA1 domain and HD domain proteins have been shown to act as cyclic di-AMP phosphodiesterases. We conclude with a consideration of the current limitations that such diversity of action places on bioinformatic prediction of the roles of GGDEF, EAL and HD-GYP domain proteins.en
dc.description.sponsorshipSvenska Forskningsrådet Formas (Swedish Research Council for Natural Sciences and Engineering (621-2013-4809)); Ministry of Education - Singapore (Tier II ARC grant); Science Foundation Ireland (SFI 07/IN.1/B955, SFI 07/IN.1/B955/IRPs, SFI 11/TIDA/B2036); Wellcome Trust (project grant WT093314MA)en
dc.description.statusPeer revieweden
dc.description.versionAccepted Versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.articleide00790-16
dc.identifier.citationRömling, U., Liang, Z.-X. and Dow, J. M. (2016) 'Progress in understanding of the molecular basis underlying functional diversification of cyclic di-nucleotide turnover proteins', Journal of Bacteriology, 199(5), e00790-16 (16pp). doi:10.1128/jb.00790-16en
dc.identifier.doi10.1128/jb.00790-16
dc.identifier.endpage16
dc.identifier.issn0021-9193
dc.identifier.issued5
dc.identifier.journaltitleJournal of Bacteriologyen
dc.identifier.startpage1
dc.identifier.urihttps://hdl.handle.net/10468/3459
dc.identifier.volume199
dc.language.isoenen
dc.publisherAmerican Society for Microbiologyen
dc.rights© 2016, American Society for Microbiology. All Rights Reserved.en
dc.subjectCyclic di-nucleotide second messengersen
dc.subjectGGDEF domainen
dc.subjectEAL domainen
dc.subjectHD-GYP domainen
dc.subjectDHH-DHHA1 proteinen
dc.titleProgress in understanding of the molecular basis underlying functional diversification of cyclic di-nucleotide turnover proteinsen
dc.typeArticle (peer-reviewed)en
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