TY - JOUR
T1 - RAD26, the yeast homolog of human Cockayne's syndrome group B gene, encodes a DNA-dependent ATPase
AU - Guzder, Sami N.
AU - Habraken, Yvette
AU - Sung, Patrick
AU - Prakash, Louise
AU - Prakash, Satya
PY - 1996
Y1 - 1996
N2 - Cells from Cockayne's syndrome (CS) patients are sensitive to ultraviolet light and defective in preferential repair of the transcribed DNA strand. CS patients suffer from complex clinical symptoms, including severe growth retardation, neurological degeneration, mental retardation, and cachexia. Two CS complementation groups, CSA and CSB, have been identified so far. RAD26 encodes the yeast counterpart of the CSB gene. Here, we purify Rad26 protein to near homogeneity from yeast cells and show that it is a DNA- dependent ATPase. In contrast to the Mfd protein that functions in transcription.coupled repair in Escherichia coli, and which is a weak and DNA independent ATPase, Rad26 is a much more active ATPase, with a strict dependence on DNA. The possible role of Rad26 ATPase in the displacement of stalled RNA polymerase II from the site of the DNA lesion and in the subsequent recruitment of a DNA repair component is discussed.
AB - Cells from Cockayne's syndrome (CS) patients are sensitive to ultraviolet light and defective in preferential repair of the transcribed DNA strand. CS patients suffer from complex clinical symptoms, including severe growth retardation, neurological degeneration, mental retardation, and cachexia. Two CS complementation groups, CSA and CSB, have been identified so far. RAD26 encodes the yeast counterpart of the CSB gene. Here, we purify Rad26 protein to near homogeneity from yeast cells and show that it is a DNA- dependent ATPase. In contrast to the Mfd protein that functions in transcription.coupled repair in Escherichia coli, and which is a weak and DNA independent ATPase, Rad26 is a much more active ATPase, with a strict dependence on DNA. The possible role of Rad26 ATPase in the displacement of stalled RNA polymerase II from the site of the DNA lesion and in the subsequent recruitment of a DNA repair component is discussed.
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U2 - 10.1074/jbc.271.31.18314
DO - 10.1074/jbc.271.31.18314
M3 - Article
C2 - 8702468
AN - SCOPUS:0029744847
SN - 0021-9258
VL - 271
SP - 18314
EP - 18317
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 31
ER -