Rescue of arrested RNA polymerase II complexes.
In the past few months, several discoveries relating to the mechanism underlying transcription-coupled DNA repair (TCR) have been reported. These results make it timely to propose a hypothesis for how eukaryotic cells might deal with arrested RNA polymerase II (Pol II) complexes. In this model, the transcription-repair coupling factor Cockayne Syndrome B (or the yeast equivalent Rad26) uses DNA translocase activity to remodel the Pol II-DNA interface, possibly to push the polymerase past the obstruction or to remove it from the DNA so that repair can take place if the obstacle is a DNA lesion. However, when this action is not possible and Pol II is left irreversibly trapped on DNA, the polymerase is instead ubiquitylated and eventually removed by proteolysis.
Svejstrup
Jesper Q
JQ
Cancer Research UK London Research Institute, Clare Hall Laboratories, South Mimms, Hertfordshire EN6 3LD, UK. j.svejstrup@cancer.org.uk
D000818:Animals; D004247:DNA / Q000235:genetics / Q000378:metabolism; D004265:DNA Helicases / Q000235:genetics; D004260:DNA Repair / Q000235:genetics*; D045643:DNA Repair Enzymes; D005057:Eukaryotic Cells / Q000201:enzymology*; D006801:Humans; D000075223:Poly-ADP-Ribose Binding Proteins; D012319:RNA Polymerase II / Q000235:genetics*; D014158:Transcription, Genetic / Q000235:genetics*; D025801:Ubiquitin / Q000378:metabolism
D000075223:Poly-ADP-Ribose Binding Proteins; D025801:Ubiquitin; D004247:DNA; D012319:RNA Polymerase II; D004265:DNA Helicases; C078673:ERCC6 protein, human; D045643:DNA Repair Enzymes