Abstract
Folding of the trigger loop of RNA polymerase promotes nucleotide addition through creating a closed, catalytically competent conformation of the active center. Here, we discuss the impact of adjacent RNA polymerase elements, including the F loop and the jaw domain, as well as external regulatory factors on the trigger loop folding and catalysis.
Keywords:
RNA polymerase; nucleotide discrimination; temperature adaptation; transcription elongation complex; trigger loop.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Biocatalysis
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DNA-Directed RNA Polymerases / chemistry*
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DNA-Directed RNA Polymerases / genetics
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DNA-Directed RNA Polymerases / metabolism*
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Models, Molecular
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Molecular Sequence Data
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Mutation
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Protein Conformation
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Protein Folding*
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Sequence Homology, Amino Acid
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Temperature
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Transcription, Genetic*
Substances
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DNA-Directed RNA Polymerases