Gulati, Abhilasha and Mahadevan, S (2001) The Escherichia coli antiterminator protein BglG stabilizes the 5’ region of the bgl mRNA. In: Journal of Biosciences, 26 (2). pp. 193-203.
The beta-glucoside utilization (bgl) genes of Escherichia coli are positively regulated by the product of the bglG gene, which functions as an antiterminator by binding to specific sequences present within the bgl mRNA. BglG is inactivated by phosphorylation in the absence of beta -glucosides by BglF, the bgl-specific component of the phosphotransferase system (PTS). Here, we present evidence for an additional function for BglG, namely the stabilization of the 5 end of the bgl mRNA. Half- life measurements of the promoter-proximal region of the bgl mRNA indicate a five fold enhancement of stability in the presence of active (unphosphorylated) BglG. This enhancement is lost when the binding of BglG to mRNA is prevented by deletion of the binding site. Interestingly, stabilization by BglG does not extend to downstream sequences. The enhanced stability of the upstream sequences suggest that BglG remains bound to its target on the mRNA even after the downstream sequences have been degraded. implications of these observations for the mechanism of positive regulation of the operon by BglG are discussed.
|Item Type:||Journal Article|
|Additional Information:||Copyright for this articles belong to the Indian Academy of Sciences.|
|Keywords:||Antitermination;mRNA stability;RNA binding protein|
|Department/Centre:||Division of Biological Sciences > Molecular Reproduction, Development & Genetics (formed by the merger of DBGL and CRBME)|
|Date Deposited:||15 Sep 2004|
|Last Modified:||19 Sep 2010 04:16|
Actions (login required)