| Literature DB >> 26527642 |
Abstract
The importance of cyclic di-GMP (c-di-GMP) and its control of biofilm matrix assembly and production has been a focal point of researchers in recent history. In this issue, Cooley et al. (Cooley RB, Smith TJ, Leung W, Tierney V, Borlee BR, O'Toole GA, Sondermann H, J Bacteriol 198:66-77, http://dx.doi.org/10.1128/JB.00369-15) demonstrate that two c-di-GMP controlled features of Pseudomonas aeruginosa, the periplasmic protease LapG and the surface adhesin CdrA, are linked. CdrA is shown to be a substrate of LapG, with LapG activity controlled by intracellular c-di-GMP levels. This commentary discusses the significance of this finding.Entities:
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Year: 2015 PMID: 26527642 PMCID: PMC4686205 DOI: 10.1128/JB.00865-15
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490