Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:6.5.1.2 (DNA ligase)
 2,749 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The bimodal-incision nature of the reaction of UV-irradiated DNA catalyzed by the Escherichia coli uvrABC protein complex potentially leads to excision of a 12- to 13-nucleotide-long damaged fragment. However, the oligonucleotide fragment containing the UV-induced pyrimidine dimer is not released under nondenaturing in vitro reaction conditions. Also, the uvrABC proteins are stably bound to the incised DNA and do not turn over after the incision event. In this communication it is shown that release of the damaged fragment from the parental uvrABC-incised DNA is dependent upon either chelating conditions or the simultaneous addition of the uvrD gene product (helicase II) and the polA gene product (DNA polymerase I) when polymerization of deoxynucleoside triphosphate substrates is concomitantly catalyzed. The product of this multiprotein-catalyzed series of reactions serves as a substrate for polynucleotide ligase, resulting in the restoration of the integrity of the strands of DNA. The addition of the uvrD protein to the incised DNA-uvrABC complex also results in turnover of the uvrC protein. It is suggested that the repair processes of incision, excision, resynthesis, and ligation are coordinately catalyzed by a complex of proteins in a "repairosome" configuration.
 ...
PMID:Involvement of helicase II (uvrD gene product) and DNA polymerase I in excision mediated by the uvrABC protein complex. 316 Oct 77

The bimodal nature of the E. coli uvrABC catalyzed incision reaction of UV irradiated DNA leads to potential excision of a 12-13 base long damaged fragment. However, the oligonucleotide fragment containing the UV-induced pyrimidine dimer is not released under non-denaturing in vitro reaction conditions. The uvrABC proteins, also, are stably bound to the incised DNA and do not turn over following the incision event. In this communication it is shown that damaged fragment release from the parental uvrABC incised DNA is dependent on either chelating conditions or upon the simultaneous addition of the uvrD gene product (helicase II) and the polA gene product (DNA polymerase I) when catalyzing concommitant polymerization of deoxynucleoside triphosphate substrates. The product of this multiprotein catalyzed series of reactions serves as a substrate for polynucleotide ligase which results in the restoration of the integrity of the strands of DNA. The addition of the uvrD protein to the incised DNA-uvrABC complex also results in turnover of only the uvrC protein. It is suggested that the repair processes of incision, excision, resynthesis and ligation are coordinately catalyzed by a protective complex of proteins in a 'repairosome' type of configuration.
 ...
PMID:The involvement of an E. coli multiprotein complex in the complete repair of UV-damaged DNA. 352 43