Chemical proteomics reveals a second family of cyclic-di-AMP hydrolases
- PMID: 25637595
- PMCID: PMC4343114
- DOI: 10.1073/pnas.1500077112
Chemical proteomics reveals a second family of cyclic-di-AMP hydrolases
Conflict of interest statement
The author declares no conflict of interest.
Comment on
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An HD-domain phosphodiesterase mediates cooperative hydrolysis of c-di-AMP to affect bacterial growth and virulence.Proc Natl Acad Sci U S A. 2015 Feb 17;112(7):E747-56. doi: 10.1073/pnas.1416485112. Epub 2015 Jan 12. Proc Natl Acad Sci U S A. 2015. PMID: 25583510 Free PMC article.
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References
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- Corrigan RM, Gründling A. Cyclic di-AMP: Another second messenger enters the fray. Nat Rev Microbiol. 2013;11(8):513–524. - PubMed
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- Witte G, Hartung S, Büttner K, Hopfner KP. Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates. Mol Cell. 2008;30(2):167–178. - PubMed
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