Backbone and nucleobase contacts to glucosamine-6-phosphate in the glmS ribozyme

Joshua A. Jansen, Tom J. McCarthy, Garrett A. Soukup, Juliane K. Soukup

Research output: Contribution to journalArticle

50 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)517-523
Number of pages7
JournalNature Structural and Molecular Biology
Volume13
Issue number6
DOIs
StatePublished - Jun 26 2006

    Fingerprint

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

Cite this