Lincoln Scott - The binding interface between Bacillus stearothermophilus ribosomal protein S15 and its 5'-translational operator mRNA.

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  Publication Details (including relevant citation   information):

  J Mol Biol. 2005   Aug 12;351(2):280-90.


  The Bacillus stearothermophilus ribosomal protein S15 (BS15)   binds a purine-rich three-helix junction motif in the central   domain of 16S ribosomal RNA (rRNA) as well as a translational   operator located in the 5'-untranslated region (5'-UTR) of its   cognate messenger RNA (mRNA). An in-frame fusion between the   5'-UTR of the BS15 gene and beta-galactosidase (lacZ) was   prepared, and tested for BS15-dependent translational repression   of lacZ activity in Escherichia coli. The presence of BS15 in   trans represses lacZ activity 24-fold. A series of detailed point   mutations in BS15 were tested for their effects upon   translational repression of lacZ activity. These point mutations   demonstrated that the 5'-UTR-BS15 binding interface utilizes many   of the same conserved amino acid residues implicated in the   binding of BS15 to 16S rRNA. The data demonstrate that the S15   protein can bind to an RNA target motif based primarily upon   appropriate minor groove and sugar-phosphate backbone contacts,   irrespective of the specific RNA sequence.

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