Abstract
The widely conserved bacterial transcription repair coupling factor (TRCF) is a large, multidomain, superfamily 2 ATPase. It couples nucleotide excision repair with transcription by dislodging inactive RNA polymerase molecules stalled at template DNA lesions and increasing the rate at which the Uvr(A)BC excinuclease acts at these sites. The recent elucidation of X-ray crystal structures of Escherichia coli TRCF revealed its architectural details, and will enable the design of more incisive experiments addressing how TRCF translocates on double-stranded DNA, destabilizes the RNA polymerase ternary elongation complex and recruits the Uvr(A)BC system.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Amino Acid Motifs
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Bacterial Proteins / chemistry*
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Bacterial Proteins / metabolism*
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Crystallography, X-Ray
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Escherichia coli Proteins / chemistry
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Escherichia coli Proteins / metabolism
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Models, Molecular
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Molecular Motor Proteins / chemistry
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Molecular Motor Proteins / metabolism
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Peptide Elongation Factors / chemistry
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Peptide Elongation Factors / metabolism
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Protein Conformation
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Transcription Factors / chemistry*
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Transcription Factors / metabolism*
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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Molecular Motor Proteins
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Peptide Elongation Factors
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Transcription Factors
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transcription repair coupling factor protein, Bacteria