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Progress in understanding of the molecular basis underlying functional diversification of cyclic di-nucleotide turnover proteins
Dow, J. Maxwell
American Society for Microbiology
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.
Cyclic di-nucleotide second messengers , GGDEF domain , EAL domain , HD-GYP domain , DHH-DHHA1 protein
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
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