دورية أكاديمية

In vitro repair of psoralen-DNA cross-links by RecA, UvrABC, and the 5'-exonuclease of DNA polymerase I.

التفاصيل البيبلوغرافية
العنوان: In vitro repair of psoralen-DNA cross-links by RecA, UvrABC, and the 5'-exonuclease of DNA polymerase I.
المؤلفون: Sladek FM; Department of Molecular Biophysics, Yale University, New Haven, Connecticut 06511., Munn MM, Rupp WD, Howard-Flanders P
المصدر: The Journal of biological chemistry [J Biol Chem] 1989 Apr 25; Vol. 264 (12), pp. 6755-65.
نوع المنشور: Journal Article; Research Support, U.S. Gov't, P.H.S.
اللغة: English
بيانات الدورية: Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print Cited Medium: Print ISSN: 0021-9258 (Print) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
أسماء مطبوعة: Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
مواضيع طبية MeSH: Cross-Linking Reagents* , DNA Damage* , DNA Repair* , Escherichia coli Proteins*, DNA/*drug effects , DNA Polymerase I/*physiology , Endodeoxyribonucleases/*physiology , Furocoumarins/*pharmacology , Rec A Recombinases/*physiology, DNA, Single-Stranded/metabolism ; Exodeoxyribonucleases/metabolism ; Recombination, Genetic
مستخلص: Psoralens produce DNA interstrand cross-links which are thought to be repaired via a sequential excision and recombination mechanism in Escherichia coli. The first round of incision by UvrABC has been characterized: it results in 11-base oligonucleotide cross-linked to an intact DNA strand (Van Houten, B., Gamper, B., Holbrook, S.R., Hearst, J.E., and Sancar, A. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 8077-8081). In the present work, DNA substrates containing 4'-hydroxymethyl-4,5',8-trimethylpsoralen (HMT) cross-links in defined positions are constructed and used to analyze the other steps in repair. It is shown that RecA protein mediates strand transfer past an oligonucleotide cross-linked to a single-stranded DNA circle and that the resulting heteroduplex is a substrate for the UvrABC complex: it excises a double-stranded oligonucleotide which contains the HMT cross-link. It is also found that the first round of UvrABC incision does not lead directly to strand exchange but that an intervening step is needed. That step is carried out in vitro by the 5'-exonuclease activity of DNA polymerase I (pol I) which creates a single-stranded DNA region (a gap) at an incised cross-link such that RecA can initiate strand exchange. Studies using cross-linked oligonucleotides showed that the gap produced by pol I results from the inability of the polymerase to add nucleotides to a 3'-OH end two to three nucleotides away from the furan side of an HMT cross-link. Pol I can, however, extend a 3'-OH end next to the pyrone side of the cross-link. Since UvrABC incises predominantly the furan side of psoralen cross-links in duplex DNA, this discrepancy has important consequences for repair.
معلومات مُعتمدة: CA39238 United States CA NCI NIH HHS; GM11014 United States GM NIGMS NIH HHS; GM31399 United States GM NIGMS NIH HHS; etc.
المشرفين على المادة: 0 (Cross-Linking Reagents)
0 (DNA, Single-Stranded)
0 (Escherichia coli Proteins)
0 (Furocoumarins)
9007-49-2 (DNA)
EC 2.7.7.- (Rec A Recombinases)
EC 2.7.7.7 (DNA Polymerase I)
EC 3.1.- (Endodeoxyribonucleases)
EC 3.1.- (Exodeoxyribonucleases)
EC 3.1.25.- (endodeoxyribonuclease uvrABC)
تواريخ الأحداث: Date Created: 19890425 Date Completed: 19890602 Latest Revision: 20220408
رمز التحديث: 20221208
PMID: 2708342
قاعدة البيانات: MEDLINE