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Titolo:
Roles of yeast DNA polymerases delta and zeta and of Rev1 in the bypass ofabasic sites
Autore:
Haracska, L; Unk, I; Johnson, RE; Johansson, E; Burgers, PMJ; Prakash, S; Prakash, L;
Indirizzi:
Univ Texas, Med Branch, Sealy Ctr Mol Sci, Galveston, TX 77555 USA Univ Texas Galveston TX USA 77555 ly Ctr Mol Sci, Galveston, TX 77555 USA Washington Univ, Sch Med, Dept Biochem & Mol Biophys, St Louis, MO 63110 USA Washington Univ St Louis MO USA 63110 Mol Biophys, St Louis, MO 63110 USA
Titolo Testata:
GENES & DEVELOPMENT
fascicolo: 8, volume: 15, anno: 2001,
pagine: 945 - 954
SICI:
0890-9369(20010415)15:8<945:ROYDPD>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
THYMINE DIMER BYPASS; SACCHAROMYCES-CEREVISIAE; REPAIR; GENE; ETA; SPECIFICITY; FIDELITY; PURIFICATION; ENDONUCLEASE; MUTAGENESIS;
Keywords:
abasic sites; mutagenic bypass; yeast; DNA polymerase delta; DNA polymerase zeta;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Prakash, L Univ Texas, Med Branch, Sealy Ctr Mol Sci, Galveston, TX 77555 USA Univ Texas Galveston TX USA 77555 Sci, Galveston, TX 77555 USA
Citazione:
L. Haracska et al., "Roles of yeast DNA polymerases delta and zeta and of Rev1 in the bypass ofabasic sites", GENE DEV, 15(8), 2001, pp. 945-954

Abstract

Abasic (AP) sites are one of the most frequently formed lesions in DNA, and they present a strong block to continued synthesis by the replicative DNAmachinery. Here we show efficient bypass of an AP site by the combined action of yeast DNA polymerases delta and zeta. In this reaction, Pol delta inserts an A nucleotide opposite the AP site, and Pol zeta subsequently extends from the inserted nucleotide. Consistent with these observations, sequence analyses of mutations in the yeast CAN1(s) gene indicate that A is the nucleotide inserted most often opposite AP sites. The nucleotides C, G, and T are also incorporated, but much less frequently. Enzymes such as Rev1 andPol eta may contribute to the insertion of these other nucleotides; the predominant role of Rev1 in AP bypass, however, is likely to be structural. Steady-state kinetic analyses show that Pol zeta is highly inefficient in incorporating nucleotides opposite the AP site, but it efficiently extends from nucleotides, particularly an A, inserted opposite this lesion. Thus, in eukaryotes, bypass of an AP site requires the sequential action of two DNA polymerases, wherein the extension step depends solely upon Pol zeta, but the insertion step can be quite varied, involving not only the predominant action of the replicative DNA polymerase, Pol delta, but also the less prominent role of various translesion synthesis polymerases.

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Documento generato il 09/04/20 alle ore 18:38:53