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Titolo:
Domain structure, localization, and function of DNA polymerase eta, defective in xeroderma pigmentosum variant cells
Autore:
Kannouche, P; Broughton, BC; Volker, M; Hanaoka, F; Mullenders, LHF; Lehmann, AR;
Indirizzi:
Univ Sussex, MRC, Cell Mutat Unit, Brighton BN1 9RR, E Sussex, England Univ Sussex Brighton E Sussex England BN1 9RR BN1 9RR, E Sussex, England Leiden Univ, Med Ctr, MGC, Dept Radiat Genet & Chem Mutagenesis, NL-2333 AL Leiden, Netherlands Leiden Univ Leiden Netherlands NL-2333 AL NL-2333 AL Leiden, Netherlands Osaka Univ, Inst Mol & Cellular Biol, Suita, Osaka 5650871, Japan Osaka Univ Suita Osaka Japan 5650871 ar Biol, Suita, Osaka 5650871, Japan
Titolo Testata:
GENES & DEVELOPMENT
fascicolo: 2, volume: 15, anno: 2001,
pagine: 158 - 172
SICI:
0890-9369(20010115)15:2<158:DSLAFO>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
THYMINE DIMER; EXCISION-REPAIR; COCKAYNES-SYNDROME; PYRIMIDINE DIMER; NUCLEAR ANTIGEN; LIGASE-I; REPLICATION; BYPASS; EXTRACTS; STRAND;
Keywords:
DNA polymerase; DNA replication; foci; translesion synthesis; UV radiation; xeroderma pigmentosum;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Lehmann, AR Univ Sussex, MRC, Cell Mutat Unit, Brighton BN1 9RR, E Sussex,England Univ Sussex Brighton E Sussex England BN1 9RR Sussex, England
Citazione:
P. Kannouche et al., "Domain structure, localization, and function of DNA polymerase eta, defective in xeroderma pigmentosum variant cells", GENE DEV, 15(2), 2001, pp. 158-172

Abstract

DNA polymerase eta carries out translesion synthesis past UV photoproductsand is deficient in xeroderma pigmentosum (XP) variants. We report that pol eta is mostly localized uniformly in the nucleus but is associated with replication foci during S phase. Following treatment of cells with UV irradiation or carcinogens, it accumulates at replication foci stalled at DNA damage. The C-terminal third of pol eta is not required for polymerase activity. However, the C-terminal 70 aa are needed for nuclear localization and a further 50 aa for relocalization into foci. Pol eta truncations lacking these domains fail to correct the defects in XP-variant cells. Furthermore, wehave identified mutations in two XP variant patients that leave the polymerase motifs intact but cause loss of the localization domains.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 15:32:14