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

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dc.contributor.author Römling, Ute
dc.contributor.author Liang, Zhao-Xun
dc.contributor.author Dow, J. Maxwell
dc.date.accessioned 2017-01-10T14:48:46Z
dc.date.available 2017-01-10T14:48:46Z
dc.date.issued 2016-12-18
dc.identifier.citation Römling, 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.00790-16 en
dc.identifier.volume 199
dc.identifier.issued 5
dc.identifier.startpage 1
dc.identifier.endpage 16
dc.identifier.issn 0021-9193
dc.identifier.uri http://hdl.handle.net/10468/3459
dc.identifier.doi 10.1128/jb.00790-16
dc.description.abstract Cyclic 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.sponsorship Svenska 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.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher American Society for Microbiology en
dc.rights © 2016, American Society for Microbiology. All Rights Reserved. en
dc.subject Cyclic di-nucleotide second messengers en
dc.subject GGDEF domain en
dc.subject EAL domain en
dc.subject HD-GYP domain en
dc.subject DHH-DHHA1 protein en
dc.title Progress in understanding of the molecular basis underlying functional diversification of cyclic di-nucleotide turnover proteins en
dc.type Article (peer-reviewed) en
dc.internal.authorcontactother Max Dow, Microbiology, University College Cork, Cork, Ireland. +353-21-490-3000 Email: m.dow@ucc.ie en
dc.internal.availability Full text available en
dc.check.info Access to this article is restricted until 6 months after publication by the request of the publisher. en
dc.check.date 2017-05-28
dc.date.updated 2017-01-10T14:30:23Z
dc.description.version Accepted Version en
dc.internal.rssid 379091563
dc.contributor.funder Svenska Forskningsrådet Formas en
dc.contributor.funder Wellcome Trust en
dc.contributor.funder Science Foundation Ireland en
dc.contributor.funder Ministry of Education - Singapore en
dc.description.status Peer reviewed en
dc.identifier.journaltitle Journal of Bacteriology en
dc.internal.copyrightchecked No !!CORA!! en
dc.internal.licenseacceptance Yes en
dc.internal.IRISemailaddress m.dow@ucc.ie en
dc.identifier.articleid e00790-16


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