Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
In eukaryotic flap endonuclease 1, the C terminus is essential for substrate binding
Autore:
Stucki, M; Jonsson, ZO; Hubscher, U;
Indirizzi:
Univ Zurich, Univ Vet Biochem, CH-8057 Zurich, Switzerland Univ Zurich Zurich Switzerland CH-8057 chem, CH-8057 Zurich, Switzerland
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 11, volume: 276, anno: 2001,
pagine: 7843 - 7849
SICI:
0021-9258(20010316)276:11<7843:IEFE1T>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL NUCLEAR ANTIGEN; STRAND DNA-SYNTHESIS; SECONDARY STRUCTURE; REPLICATION FORK; EXCISION-REPAIR; FEN-1; PCNA; COMPLEX; INHIBITION; EXPANSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Hubscher, U Univ Zurich, Univ Vet Biochem, Winterthurerstr 190, CH-8057 Zurich, Switzerland Univ Zurich Winterthurerstr 190 Zurich Switzerland CH-8057 nd
Citazione:
M. Stucki et al., "In eukaryotic flap endonuclease 1, the C terminus is essential for substrate binding", J BIOL CHEM, 276(11), 2001, pp. 7843-7849

Abstract

Flap endonuclease 1 (Fen1) is a structure-specific metallonuclease with important functions in DNA replication and DNA repair. It interacts like manyother proteins involved in DNA metabolic events with proliferating cell nuclear antigen (PCNA), and its enzymatic activity is stimulated by PCNA in vitro. The PCNA interaction site is located close to the C terminus of Fen1 and is flanked by a conserved basic region of 35-38 amino acids in eukaryotic species but not in archaea. We have constructed two deletion mutants of human Fen1 that lack either the PCNA interaction motif or a part of its adjacent C-terminal region and analyzed them in a variety of assays. Remarkably, deletion of the basic C-terminal region did not affect PCNA interaction but resulted in a protein with significantly reduced enzymatic activity. Electrophoretic mobility shift analysis revealed that this mutant displayed asevere defect in substrate binding. Our results suggest that the C terminus of eukaryotic Fen1 consists of two functionally distinct regions that together might form an important regulatory domain.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 17:07:40