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Titolo:
THE 1ST ZINC-BINDING DOMAIN OF UVRA IS NOT ESSENTIAL FOR UVRABC-MEDIATED DNA EXCISION-REPAIR
Autore:
VISSE R; DERUIJTER M; UBBINK M; BRANDSMA JA; VANDEPUTTE P;
Indirizzi:
LEIDEN UNIV,GORLAEUS LABS,DEPT BIOCHEM,MOLEC GENET LAB,POB 9502 2300 RA LEIDEN NETHERLANDS
Titolo Testata:
MUTATION RESEARCH
fascicolo: 3, volume: 294, anno: 1993,
pagine: 263 - 274
SICI:
0027-5107(1993)294:3<263:T1ZDOU>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI UVRA; SITE-SPECIFIC MUTAGENESIS; POLY(ADP-RIBOSE) POLYMERASE; REGULATORY PROTEIN; BACTERIOPHAGE-MU; FINGER; ENDONUCLEASE; COMPLEX; MOTIF; TRANSPOSITION;
Keywords:
DNA REPAIR; UVRABC ENDONUCLEASE; ZINC BINDING DOMAINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
41
Recensione:
Indirizzi per estratti:
Citazione:
R. Visse et al., "THE 1ST ZINC-BINDING DOMAIN OF UVRA IS NOT ESSENTIAL FOR UVRABC-MEDIATED DNA EXCISION-REPAIR", MUTATION RESEARCH, 294(3), 1993, pp. 263-274

Abstract

Specific mutations in uvrA were introduced to analyze the role of thezinc-binding domains of the protein in DNA excision repair. Zinc-coordinating cysteines were substituted into non-coordinating serine or glycine residues. Mutations leading to changes in the second zinc-binding domain had a profound effect on UV survival in vivo; however these mutant proteins could not be isolated for in vitro analyses. Amino acidsubstitutions in the first zinc-binding domain had very little effecton UV survival in vivo. In vitro analyses showed that although this domain no longer coordinates zinc, ATPase activity, helicase activity, DNA binding, incision of damaged DNA and DNA repair synthesis appearedto be normal. Therefore it seems that the first zinc-binding domain of UvrA is not essential for DNA excision repair.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 10:38:44