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 language | English |
|---|---|
| Pages (from-to) | 517-523 |
| Number of pages | 7 |
| Journal | Nature Structural and Molecular Biology |
| Volume | 13 |
| Issue number | 6 |
| DOIs | |
| State | Published - Jun 26 2006 |
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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 journal › Article
}
TY - JOUR
T1 - Backbone and nucleobase contacts to glucosamine-6-phosphate in the glmS ribozyme
AU - Jansen, Joshua A.
AU - McCarthy, Tom J.
AU - Soukup, Garrett
AU - Strauss-Soukup, Juliane K.
PY - 2006/6/26
Y1 - 2006/6/26
N2 - 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.
AB - 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.
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U2 - 10.1038/nsmb1094
DO - 10.1038/nsmb1094
M3 - Article
VL - 13
SP - 517
EP - 523
JO - Nature Structural and Molecular Biology
JF - Nature Structural and Molecular Biology
SN - 1545-9993
IS - 6
ER -