Autor: |
Lalaouna, David, Morissette, Audrey, Carrier, Marie‐Claude, Massé, Eric |
Předmět: |
|
Zdroj: |
Molecular Microbiology; Oct2015, Vol. 98 Issue 2, p357-369, 13p, 2 Diagrams, 7 Graphs |
Abstrakt: |
The 87 nucleotide long DsrA s RNA has been mostly studied for its translational activation of the transcriptional regulator RpoS. However, it also represses hns m RNA, which encodes H- NS, a major regulator that affects expression of nearly 5% of E scherichia coli genes. A speculative model previously suggested that DsrA would block hns m RNA translation by binding simultaneously to start and stop codon regions of hns m RNA (coaxial model). Here, we show that DsrA efficiently blocked translation of hns m RNA by base-pairing immediately downstream of the start codon. In addition, DsrA induced hns m RNA degradation by actively recruiting the RNA degradosome complex. Data presented here led to a model of DsrA action on hns m RNA, which supports a canonical mechanism of s RNA-induced m RNA degradation by binding to the translation initiation region. Furthermore, using MS2-affinity purification coupled with RNA sequencing technology (MAPS), we also demonstrated that DsrA targets rbs D m RNA, involved in ribose utilization. Surprisingly, DsrA base pairs far downstream of rbs D start codon and induces rapid degradation of the transcript. Thus, our study enables us to draw an extended DsrA targetome. [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
Externí odkaz: |
|