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McClellanville Library
9 a.m. - 1 p.m.
Phone: (843) 887-3699
Folly Beach Library
9 a.m. - 1 p.m.
Phone: (843) 588-2001
Miss Jane's Building (Edisto Library Temporary Location)
9 a.m. – 3 p.m.
Phone: (843) 869-2355
Main Library
9 a.m. - 6 p.m.
Phone: (843) 805-6930
West Ashley Library
9 a.m. - 4 p.m.
Phone: (843) 766-6635
John L. Dart Library
9 a.m. - 6 p.m.
Phone: (843) 722-7550
St. Paul's/Hollywood Library
9 a.m. - 5 p.m.
Phone: (843) 889-3300
Mt. Pleasant Library
9 a.m. – 6 p.m.
Phone: (843) 849-6161
Dorchester Road Library
9 a.m. - 6 p.m.
Phone: (843) 552-6466
Edgar Allan Poe/Sullivan's Island Library
9 a.m. - 6 p.m.
Phone: (843) 883-3914
John's Island Library
9 a.m. - 6 p.m.
Phone: (843) 559-1945
Wando Mount Pleasant Library
9 a.m. - 6 p.m.
Phone: (843) 805-6888
Otranto Road Library
9 a.m. - 6 p.m.
Phone: (843) 572-4094
Hurd/St. Andrews Library
9 a.m. - 6 p.m.
Phone: (843) 766-2546
Baxter-Patrick James Island
9 a.m. - 6 p.m.
Phone: (843) 795-6679
Bees Ferry West Ashley Library
9 a.m. - 6 p.m.
Phone: (843) 805-6892
Village Library
9 a.m. - 6 p.m.
Phone: (843) 884-9741
Keith Summey North Charleston Library
9 a.m. – 6 p.m.
Phone: (843) 744-2489
Mobile Library
9 a.m. - 5 p.m.
Phone: (843) 805-6909
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Initiation of transcription-coupled repair characterized at single-molecule resolution.
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- Author(s): Howan, Kévin; Smith, Abigail J.; Westblade, Lars F.; Joly, Nicolas; Grange, Wilfried; Zorman, Sylvain; Darst, Seth A.; Savery, Nigel J.; Strick, Terence R.
- Source:
Nature; 10/18/2012, Vol. 490 Issue 7420, p431-434, 4p, 1 Diagram, 3 Graphs- Subject Terms:
- Source:
- Additional Information
- Abstract: Transcription-coupled DNA repair uses components of the transcription machinery to identify DNA lesions and initiate their repair. These repair pathways are complex, so their mechanistic features remain poorly understood. Bacterial transcription-coupled repair is initiated when RNA polymerase stalled at a DNA lesion is removed by Mfd, an ATP-dependent DNA translocase. Here we use single-molecule DNA nanomanipulation to observe the dynamic interactions of Escherichia coli Mfd with RNA polymerase elongation complexes stalled by a cyclopyrimidine dimer or by nucleotide starvation. We show that Mfd acts by catalysing two irreversible, ATP-dependent transitions with different structural, kinetic and mechanistic features. Mfd remains bound to the DNA in a long-lived complex that could act as a marker for sites of DNA damage, directing assembly of subsequent DNA repair factors. These results provide a framework for considering the kinetics of transcription-coupled repair in vivo, and open the way to reconstruction of complete DNA repair pathways at single-molecule resolution. [ABSTRACT FROM AUTHOR]
- Abstract:
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