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Titolo:
Physical and functional interactions of human DNA polymerase eta with PCNA
Autore:
Haracska, L; Johnson, RE; Unk, I; Phillips, B; Hurwitz, J; Prakash, L; Prakash, S;
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 Mem Sloan Kettering Canc Ctr, Dept Mol Biol & Virol, Ctr Canc, New York, NY 10021 USA Mem Sloan Kettering Canc Ctr New York NY USA 10021 New York, NY 10021 USA
Titolo Testata:
MOLECULAR AND CELLULAR BIOLOGY
fascicolo: 21, volume: 21, anno: 2001,
pagine: 7199 - 7206
SICI:
0270-7306(200111)21:21<7199:PAFIOH>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL NUCLEAR ANTIGEN; PIGMENTOSUM VARIANT CELLS; THYMINE-THYMINE DIMER; SACCHAROMYCES-CEREVISIAE; XERODERMA-PIGMENTOSUM; POSTREPLICATION REPAIR; MUTATION SPECTRA; REPLICATION; FIDELITY; YEAST;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Prakash, S Univ Texas, Med Branch, Sealy Ctr Mol Sci, 6-104 Blocker Med Res Bldg,11th& Mech St, Galveston, TX 77555 USA Univ Texas 6-104 Blocker Med Res Bldg,11th & Mech St Galveston TX USA 77555
Citazione:
L. Haracska et al., "Physical and functional interactions of human DNA polymerase eta with PCNA", MOL CELL B, 21(21), 2001, pp. 7199-7206

Abstract

Human DNA polymerase eta (hPol eta) functions in the error-free replication of UV-damaged DNA, and mutations in hPol eta cause cancer-prone syndrome,the variant form of xeroderma pigmentosum. However, in spite of its key role in promoting replication through a variety of distorting DNA lesions, the manner by which hPol eta is targeted to the replication machinery stalledat a lesion site remains unknown. Here, we provide evidence for the physical interaction of hPol eta with proliferating cell nuclear antigen (PCNA) and show that mutations in the PCNA binding motif of hPol eta inactivate this interaction. PCNA, together with replication factor C and replication protein A, stimulates the DNA synthetic activity of hPol eta, and steady-statekinetic studies indicate that this stimulation accrues from an increase inthe efficiency of nucleotide insertion resulting from a reduction in the apparent K-m for the incoming nucleotide.

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Documento generato il 02/04/20 alle ore 22:20:56