PMID- 2775737
OWN - NLM
STAT- MEDLINE
DCOM- 19891026
LR  - 20190613
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 28
IP  - 14
DP  - 1989 Jul 11
TI  - Recognition and repair of 2-aminofluorene- and 2-(acetylamino)fluorene-DNA 
      adducts by UVRABC nuclease.
PG  - 5821-6
AB  - Recognition of damage induced by N-hydroxy-2-aminofluorene (N-OH-AF) and 
      N-acetoxy-2-(acetylamino)fluorene (NAAAF) in both phi X174 RFI supercoiled DNA 
      and a linear DNA fragment by purified UVRA, UVRB, and UVRC proteins was 
      investigated. We have previously demonstrated that N-OH-AF and NAAAF treatments 
      produce N-(deoxyguanosin-8-yl)-2-aminofluorene (dG-C8-AF) and 
      N-(deoxyguanosin-8-yl)-2-(acetylamino)fluorene (dG-C8-AAF), respectively, in DNA. 
      Using a piperidine cleavage method and DNA sequence analysis, we have found that 
      all guanine residues can be modified by N-OH-AF and NAAAF. These two kinds of 
      adducts have different impacts on the DNA helix structure; while dG-C8-AF 
      maintains the anti configuration, dG-C8-AAF is in the syn form. phi X174 RF 
      DNA-Escherichia coli transfection results indicate that while the uvrA, uvrB, and 
      uvrC gene products are needed to repair dG-C8-AAF, the uvrC, but not the uvrA or 
      uvrB gene products, is needed for repair of dG-C8-AF. However, we have found that 
      in vitro the UVRA, UVRB, and UVRC proteins must work in concert to nick both 
      dG-C8-AF and dG-C8-AAF. In general, the reactions of UVRABC nuclease toward 
      dG-C8-AF are similar to those toward dG-C8-AAF; it incises seven to eight 
      nucleotides from the 5' side and three to four nucleotides from the 3' side of 
      the DNA adduct. Evidence is presented to suggest that hydrolysis on the 3' and 5' 
      sides of the damaged base by UVRABC nuclease is not simultaneous and that at 
      least occasionally hydrolysis occurs only on the 3' side or on the 5' side of the 
      damage site. The possible mechanisms of UVRABC nuclease incision for AF-DNA are 
      discussed.
FAU - Pierce, J R
AU  - Pierce JR
AD  - M. D. Anderson Cancer Center, Science Park-Research Division, University of 
      Texas, Smithville 78957.
FAU - Case, R
AU  - Case R
FAU - Tang, M S
AU  - Tang MS
LA  - eng
GR  - CA 09480-05/CA/NCI NIH HHS/United States
GR  - CA 42897/CA/NCI NIH HHS/United States
GR  - ES 031124/ES/NIEHS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Escherichia coli Proteins)
RN  - 0 (Fluorenes)
RN  - 3A69OS195N (2-aminofluorene)
RN  - 9007-49-2 (DNA)
RN  - 9M98QLJ2DL (2-Acetylaminofluorene)
RN  - EC 3.1.- (Endodeoxyribonucleases)
RN  - EC 3.1.25.- (endodeoxyribonuclease uvrABC)
SB  - IM
MH  - 2-Acetylaminofluorene/metabolism
MH  - DNA/metabolism
MH  - *DNA Repair
MH  - Endodeoxyribonucleases/*metabolism
MH  - *Escherichia coli Proteins
MH  - Fluorenes/metabolism
MH  - Hydrolysis
MH  - Nucleic Acid Conformation
EDAT- 1989/07/11 00:00
MHDA- 1989/07/11 00:01
CRDT- 1989/07/11 00:00
PHST- 1989/07/11 00:00 [pubmed]
PHST- 1989/07/11 00:01 [medline]
PHST- 1989/07/11 00:00 [entrez]
AID - 10.1021/bi00440a018 [doi]
PST - ppublish
SO  - Biochemistry. 1989 Jul 11;28(14):5821-6. doi: 10.1021/bi00440a018.