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Titolo:
Human homolog of the MutY repair protein (hMYH) physically interacts with proteins involved in long patch DNA base excision repair
Autore:
Parker, A; Gu, YS; Mahoney, W; Lee, SH; Singh, KK; Lu, AL;
Indirizzi:
Univ Maryland, Dept Biochem & Mol Biol, Baltimore, MD 21201 USA Univ Maryland Baltimore MD USA 21201 & Mol Biol, Baltimore, MD 21201 USA Univ Maryland, Combined PhD Program Biochem, Baltimore, MD 21201 USA Univ Maryland Baltimore MD USA 21201 ram Biochem, Baltimore, MD 21201 USA Indiana Univ, Ctr Canc, Dept Biochem & Mol Biol, Indianapolis, IN 46202 USA Indiana Univ Indianapolis IN USA 46202 l Biol, Indianapolis, IN 46202 USA Indiana Univ, Sch Med, Walther Oncol Ctr, Indianapolis, IN 46202 USA Indiana Univ Indianapolis IN USA 46202 ol Ctr, Indianapolis, IN 46202 USA Johns Hopkins Oncol Ctr, Radiat Res Program, Baltimore, MD 21231 USA JohnsHopkins Oncol Ctr Baltimore MD USA 21231 m, Baltimore, MD 21231 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 8, volume: 276, anno: 2001,
pagine: 5547 - 5555
SICI:
0021-9258(20010223)276:8<5547:HHOTMR>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL NUCLEAR ANTIGEN; PURIFIED HUMAN PROTEINS; POLYMERASE-BETA; MAMMALIAN-CELLS; MISMATCH REPAIR; LIGASE-I; SCHIZOSACCHAROMYCES-POMBE; SACCHAROMYCES-CEREVISIAE; FUNCTIONAL EXPRESSION; MOLECULAR-CLONING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
73
Recensione:
Indirizzi per estratti:
Indirizzo: Lu, AL Univ Maryland, Dept Biochem & Mol Biol, 108 N Greene St, Baltimore,MD 21201 USA Univ Maryland 108 N Greene St Baltimore MD USA 21201 , MD 21201 USA
Citazione:
A. Parker et al., "Human homolog of the MutY repair protein (hMYH) physically interacts with proteins involved in long patch DNA base excision repair", J BIOL CHEM, 276(8), 2001, pp. 5547-5555

Abstract

The human MutY homolog (hMYH) is a DNA glycosylase involved in the removalof adenines or 2-hydroxyadenines misincorporated with template guanines or7,8-dihydro-8-oxodeoxyguanines. hMYH is associated in vivo with apurinic/apyrimidinic endonuclease (APE1), proliferating cell nuclear antigen (PCNA),and replication protein A (RPA) in HeLa nuclear extracts as shown by immunoprecipitation and Western blotting. However, binding of hMYH to DNA polymerases beta and delta was not detected. By using constructs containing different portions of hMYH fused to glutathione S-transferase, we have demonstrated that the APE1-binding site is at a region around amino acid residue 300, that the PCNA binding activity is located at the C terminus, and that RPAbinds to the N terminus of hMYH. A peptide consisting of residues 505-527 of hMYH that contains a conserved PCNA-binding motif binds PCNA, and subsequent amino acid substitution identified Phe-518 and Phe-519 as essential residues required for PCNA binding. RPA binds to a peptide that consists of residues 6-32 of hMYH and contains a conserved RPA-binding motif. The PCNA- and RPA-binding sites of hMYH are further confirmed by peptide and antibodytitration. These results suggest that hMYH repair is a long patch base excision repair pathway.

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Documento generato il 23/11/20 alle ore 20:24:06