Lincoln Scott - Interaction of the Bacillus stearothermophilus ribosomal protein S15 with its 5'-translational operator mRNA.

Version 1

      Publication Details (including relevant citation   information):

      J Mol Biol. 2001   Nov 30;314(3):413-22.

      Abstract:

      The Bacillus stearothermophilus ribosomal protein S15 (BS15)   binds both a three-helix junction in the central domain of 16 S   ribosomal RNA and its cognate mRNA. Native gel mobility-shift   assays show that BS15 interacts specifically and with high   affinity to the 5'-untranslated region (5'-UTR) of this cognate   mRNA with an apparent dissociation constant of 3(+/-0.3) nM. In   order to localize the structural elements that are essential for   BS15 recognition, a series of deletion mutants of the full   cognate mRNA were prepared and tested in the same gel-shift   assay. The minimal binding site for BS15 is a 50 nucleotide RNA   showing a close secondary structure resemblance to the BS15   binding region from 16 S rRNA. There are two major structural   motifs that must be maintained for high-affinity binding. The   first being a purine-rich three-helix junction, and the second   being an internal loop. The sequence identity of the internal   loops differs greatly between the BS15 mRNA and rRNA sites, and   this difference is correlated to discrimination between wild-type   BS15 and a BS15(H45R) mutant. The association and dissociation   kinetics measured for the 5'-UTR-BS15 interaction are quite slow,   but are typical for a ribosomal protein-RNA interaction. The BS15   mRNA and 16 S rRNA binding sites share a common secondary   structure yet have little sequence identity. The mRNA and rRNA   may in fact present similar if not identical structural elements   that confer BS15 recognition.

      Address (URL): http://www.ncbi.nlm.nih.gov/pubmed/11846555