We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Backbone and nucleobase contacts to glucosamine-6-phosphate in the glmS ribozyme.
- Authors
Jansen, Joshua A; McCarthy, Tom J; Soukup, Garrett A; Soukup, Juliane K
- Abstract
The glmS ribozyme resides in the 5' untranslated region of glmS mRNA and functions as a catalytic riboswitch that regulates amino sugar metabolism in certain Gram-positive bacteria. The ribozyme catalyzes self-cleavage of the mRNA and ultimately inhibits gene expression in response to binding of glucosamine-6-phosphate (GlcN6P), the metabolic product of the GlmS protein. We have used nucleotide analog interference mapping (NAIM) and suppression (NAIS) to investigate backbone and nucleobase functional groups essential for ligand-dependent ribozyme function. NAIM using GlcN6P as ligand identified requisite structural features and potential sites of ligand and/or metal ion interaction, whereas NAIS using glucosamine as ligand analog revealed those sites that orchestrate recognition of ligand phosphate. These studies demonstrate that the ligand-binding site lies in close proximity to the cleavage site in an emerging model of ribozyme structure that supports a role for ligand within the catalytic core.
- Publication
Nature structural & molecular biology, 2006, Vol 13, Issue 6, p517
- ISSN
1545-9993
- Publication type
Journal Article
- DOI
10.1038/nsmb1094