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Titolo:
THE YEAST 8-OXOGUANINE DNA GLYCOSYLASE (OGG1) CONTAINS A DNA DEOXYRIBOPHOSPHODIESTERASE (DRPASE) ACTIVITY
Autore:
SANDIGURSKY M; YACOUB A; KELLEY MR; XU Y; FRANKLIN WA; DEUTSCH WA;
Indirizzi:
LOUISIANA STATE UNIV,PENNINGTON BIOMED RES CTR BATON ROUGE LA 70808 LOUISIANA STATE UNIV,PENNINGTON BIOMED RES CTR BATON ROUGE LA 70808 YESHIVA UNIV ALBERT EINSTEIN COLL MED,DEPT RADIAT ONCOL BRONX NY 10461 YESHIVA UNIV ALBERT EINSTEIN COLL MED,DEPT RADIOL BRONX NY 10461 INDIANA UNIV,SCH MED,DEPT BIOCHEM & MOL BIOL INDIANAPOLIS IN 46202 INDIANA UNIV,SCH MED,WELLS CTR PEDIAT RES,DEPT PEDIAT,SECT PEDIAT ENDOCRINOL INDIANAPOLIS IN 46202
Titolo Testata:
Nucleic acids research
fascicolo: 22, volume: 25, anno: 1997,
pagine: 4557 - 4561
SICI:
0305-1048(1997)25:22<4557:TY8DG(>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
APURINIC APYRIMIDINIC SITES; ESCHERICHIA-COLI; G.C->T.A TRANSVERSIONS; DEOXYRIBOSE PHOSPHATE; EXONUCLEASE-I; PROTEIN; REPAIR; 8-HYDROXYGUANINE; EXCISION; ENDONUCLEASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
24
Recensione:
Indirizzi per estratti:
Citazione:
M. Sandigursky et al., "THE YEAST 8-OXOGUANINE DNA GLYCOSYLASE (OGG1) CONTAINS A DNA DEOXYRIBOPHOSPHODIESTERASE (DRPASE) ACTIVITY", Nucleic acids research, 25(22), 1997, pp. 4557-4561

Abstract

The yeast OGG1 gene was recently cloned and shown to encode a proteinthat possesses N-glycosylase/AP lyase activities for the repair of oxidatively damaged DNA at sites of 7, 8-dihydro-8-oxoguanine (8-oxoguanine). Similar activities have been identified for Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg) and Drosophila ribosomal protein S3. Both Fpg and S3 also contain a deoxyribophosphodiesterase (dRpase) activity. that removes 2-deoxyribose-5-phosphate at an incised 5' apurinic/apyrimidinic (AP) sites via a beta-elimination reaction. Drosophila S3 also has an additional activity that removes trans-4-hydroxy-2-pentenal-5-phosphate at a 3' incised AP site by a Mg2+-dependent hydrolytic mechanism, In view of the substrate similarities between Ogg1,Fpg and S3 at the level of base excision repair, we examined whether Ogg1 also contains dRpase activities. A glutathione S-transferase fusion protein of Ogg1 was purified and subsequently found to efficiently remove sugar-phosphate residues at incised 5' AP sites. Activity was also detected for the Mg2+-dependent removal of trans-4-hydroxy-2-pentenal-5-phosphate at 3' incised AP sites and from intact AP sites. Previous studies have shown that DNA repair proteins that possess AP lyase activity leave an inefficient DNA terminus for subsequent DNA synthesis steps associated with base excision repair. However, the results presented here suggest that in the presence of MgCl2, Ogg1 can efficiently process 8-oxoguanine so as to leave a one nucleotide gap that can bereadily filled in by a DNA polymerase, and importantly, does not therefore require additional enzymes to process trans-4-hydroxy-2-pentenal-5-phosphate left at a 3' terminus created by a p-elimination catalyst.

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Documento generato il 05/12/20 alle ore 01:04:31