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Titolo:
FUNCTIONAL COMPLEMENTATION OF XERODERMA-PIGMENTOSUM COMPLEMENTATION GROUP-E BY REPLICATION PROTEIN-A IN AN IN-VITRO SYSTEM
Autore:
KAZANTSEV A; MU D; NICHOLS AF; ZHAO XD; LINN S; SANCAR A;
Indirizzi:
UNIV N CAROLINA,SCH MED,DEPT BIOCHEM & BIOPHYS CHAPEL HILL NC 27599 UNIV CALIF BERKELEY,DIV BIOCHEM & MOLEC BIOL BERKELEY CA 94720
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 10, volume: 93, anno: 1996,
pagine: 5014 - 5018
SICI:
0027-8424(1996)93:10<5014:FCOXCG>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
DNA-BINDING-PROTEIN; NUCLEOTIDE EXCISION NUCLEASE; SIMIAN VIRUS-40 DNA; DAMAGED DNA; SUBUNIT; REPAIR; EXTRACT; INVITRO;
Keywords:
DNA REPAIR; DAMAGE RECOGNITION; EXCISION NUCLEASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
A. Kazantsev et al., "FUNCTIONAL COMPLEMENTATION OF XERODERMA-PIGMENTOSUM COMPLEMENTATION GROUP-E BY REPLICATION PROTEIN-A IN AN IN-VITRO SYSTEM", Proceedings of the National Academy of Sciences of the United Statesof America, 93(10), 1996, pp. 5014-5018

Abstract

Xeroderma pigmentosum (XP) is caused by a defect in nucleotide excision repair. Patients in the complementation group E (XP-E) have the mildest form of the disease and the highest level of residual repair activity. About 20% of the cell strains derived from XP-E patients lack a damaged DNA-binding protein (DDB) activity that binds to ultraviolet-induced (6-4) photoproducts with high affinity. We report here that cell-free extracts prepared from XP-E cell strains that either lacked or contained DDB activity were severely defective in excising DNA damage including (6-4) photoproducts. However, this excision activity defect was not restored by addition of purified DDB that. In fact, inhibited removal of (6-4) photoproducts by the human excision nuclease reconstituted from purified proteins. Extensive purification of correcting activity from HeLa cells revealed that the correcting activity is inseparable from the human replication/repair protein A [RPA (also known as human single stranded DNA binding protein, HSSB)]. Indeed, supplementing XP-E extracts with recombinant human RPA purified from Escherichia coli restored excision activity. However, no mutation was found in the genes encoding the three subunits of RPA in an XP-E (DDB-) cell line. It is concluded that RPA functionally complements XP-E extracts in vitro, but it is not genetically altered in XP-E patients.

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Documento generato il 25/01/20 alle ore 16:20:57