This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Structural basis for bacterial transcription coupled repair - TRCF(Transcription Repair Coupling Factor) is a widely conserved bacterial protein that couples DNA repair with transcription. TRCF recognizes RNA polymerase (RNAP) stalled at a non-coding template site of DNA damage, disrupts the transcription complex, and recruits the DNA excision repair machinery to the site. The mechanism of RNA release has been illuminated by the discovery that TRCF causes forward translocation of RNAP, using an ATP-dependent motor that is homologous to that of the Holliday branch migration protein RecG. TRCF is a large (130 kD) protein with a complex structure/function relationship that is not understood. We have undertaken detailed structural studies to elucidate the structure/function relationship of TRCF, to reveal conformational changes involved in the ATP-hydrolysis cycle and its coupling to the DNA translocase activity, and to reveal the interactions of TRCF with the transcription comp
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