dc.contributor.author |
Römling, Ute |
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dc.contributor.author |
Liang, Zhao-Xun |
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dc.contributor.author |
Dow, J. Maxwell |
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dc.date.accessioned |
2017-01-10T14:48:46Z |
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dc.date.available |
2017-01-10T14:48:46Z |
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dc.date.issued |
2016-12-18 |
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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 |
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dc.identifier.issued |
5 |
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dc.identifier.startpage |
1 |
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dc.identifier.endpage |
16 |
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dc.identifier.issn |
0021-9193 |
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dc.identifier.uri |
http://hdl.handle.net/10468/3459 |
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dc.identifier.doi |
10.1128/jb.00790-16 |
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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 |
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dc.date.updated |
2017-01-10T14:30:23Z |
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dc.description.version |
Accepted Version |
en |
dc.internal.rssid |
379091563 |
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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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