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

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

Research output: Contribution to journalArticle

48 Citations (Scopus)

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

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Catalytic RNA
Ligands
Nucleotides
Riboswitch
Amino Sugars
Messenger RNA
5' Untranslated Regions
Glucosamine
Gram-Positive Bacteria
glucosamine 6-phosphate
Catalytic Domain
Metals
Phosphates
Binding Sites
Ions
Gene Expression

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Structural Biology

Cite this

Backbone and nucleobase contacts to glucosamine-6-phosphate in the glmS ribozyme. / Jansen, Joshua A.; McCarthy, Tom J.; Soukup, Garrett; Strauss-Soukup, Juliane K.

In: Nature Structural and Molecular Biology, Vol. 13, No. 6, 26.06.2006, p. 517-523.

Research output: Contribution to journalArticle

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