Abstract
The exact mechanism by which cellular RNA polymerases translocate and maintain exceptionally high fidelity during transcription remains a major unresolved issue. Two recent structural studies of yeast RNA polymerase II in complex with its potent inhibitor, the fungal toxin α-amanitin, address this matter by describing critical and surprising details about the enzyme catalytic center dynamic organization.
Publication types
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Comment
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News
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Research Support, N.I.H., Extramural
MeSH terms
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Alpha-Amanitin / chemistry
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DNA / chemistry
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Fungal Proteins / chemistry
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Gene Deletion
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Models, Biological
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Models, Molecular
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Nucleotides / chemistry
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Protein Conformation
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Protein Structure, Secondary
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Protein Transport
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RNA Polymerase II / metabolism*
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Transcription, Genetic*
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Yeasts
Substances
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Alpha-Amanitin
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Fungal Proteins
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Nucleotides
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DNA
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RNA Polymerase II