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Regulation of CsrB/C sRNA decay by EIIA Glc of the phosphoenolpyruvate: carbohydrate phosphotransferase system
Author(s) -
Leng Yuanyuan,
Vakulskas Christopher A.,
Zere Tesfalem R.,
Pickering Bradley S.,
Watnick Paula I.,
Babitzke Paul,
Romeo Tony
Publication year - 2016
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.13259
Subject(s) - biology , pep group translocation , translation (biology) , microbiology and biotechnology , rna , rnase p , messenger rna , gene , phosphoenolpyruvate carboxykinase , biochemistry
Summary Csr is a conserved global regulatory system, which uses the sequence‐specific RNA ‐binding protein CsrA to activate or repress gene expression by binding to m RNA and altering translation, stability and/or transcript elongation. In E scherichia coli , CsrA activity is regulated by two s RNA s, CsrB and CsrC , which bind to multiple CsrA dimers, thereby sequestering this protein away from its mRNA targets. Turnover of CsrB / C s RNA s is tightly regulated by a GGDEF‐EAL domain protein, CsrD , which targets them for cleavage by RN ase E . Here, we show that EIIA Glc of the glucose‐specific PTS system is also required for the normal decay of these s RNA s and that it acts by binding to the EAL domain of CsrD . Only the unphosphorylated form of EIIA Glc bound to CsrD in vitro and was capable of activating CsrB / C turnover in vivo . Genetic studies confirmed that this mechanism couples CsrB / C s RNA decay to the availability of a preferred carbon source. These findings reveal a new physiological influence on the workings of the C sr system, a novel function for the EAL domain, and an important new way in which EIIA Glc shapes global regulatory circuitry in response to nutritional status.