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Titolo:
A novel nuclear export signal sensitive to oxidative stress in the fissionyeast transcription factor Pap1
Autore:
Kudo, N; Taoka, H; Toda, T; Yoshida, M; Horinouchi, S;
Indirizzi:
Univ Tokyo, Grad Sch Agr & Life Sci, Dept Biotechnol, Bunkyo Ku, Tokyo 113, Japan Univ Tokyo Tokyo Japan 113 Dept Biotechnol, Bunkyo Ku, Tokyo 113, Japan Imperial Canc Res Fund, Lab Cell Regulat, London WC2A 3PX, England Imperial Canc Res Fund London England WC2A 3PX London WC2A 3PX, England
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 21, volume: 274, anno: 1999,
pagine: 15151 - 15158
SICI:
0021-9258(19990521)274:21<15151:ANNESS>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
ORDER CHROMOSOME STRUCTURE; BREFELDIN-A RESISTANCE; REV ACTIVATION DOMAIN; SCHIZOSACCHAROMYCES-POMBE; LEPTOMYCIN-B; SACCHAROMYCES-CEREVISIAE; MAP KINASE; CELL-CYCLE; NUCLEOCYTOPLASMIC TRANSPORT; MUTATIONAL ANALYSIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
61
Recensione:
Indirizzi per estratti:
Indirizzo: Yoshida, M Univ Tokyo, Grad Sch Agr & Life Sci, Dept Biotechnol, Bunkyo Ku, Tokyo 113, Japan Univ Tokyo Tokyo Japan 113 chnol, Bunkyo Ku, Tokyo 113, Japan
Citazione:
N. Kudo et al., "A novel nuclear export signal sensitive to oxidative stress in the fissionyeast transcription factor Pap1", J BIOL CHEM, 274(21), 1999, pp. 15151-15158

Abstract

Pap1, a fission yeast AP-l-like transcription factor, is negatively regulated by CRM1/exportin 1, the nuclear export factor. Pap1 was localized normally in the cytoplasm but was accumulated in the nucleus when Crm1 was inactivated by a temperature sensitive mutation or by treatment with leptomycin B, a specific export inhibitor. Deletion of the C-terminal cysteine-rich domain (CRD) resulted in nuclear accumulation of Pap1, while a glutathione S-transferase-green fluorescent protein-CRD fusion protein was localized in the cytoplasm in a Crm1-dependent manner. Deletion and mutational analyses identified several important amino acids in a 19-amino acid region in the CRD as a nuclear export signal (NES), Strikingly, a cysteine residue (Cys-532), in addition to two leucines and an isoleucine, was important for the NESfunction and the presence of at least one of the two cysteine residues wasessential. Unlike classical NESs such as the human immunodeficiency virus Rev NES, the Pap1 NES lost the function upon treatment with oxidants such as diethyl maleate. The oxidative stress response is conserved through evolution, as green fluorescent protein-fused proteins bearing the Pap1 NES expressed in mammalian cells responded to diethyl maleate. These results show that the hydrophobic amino acid-rich region containing two important cysteines in Pap1 serves as a novel NES, which is sensitive to oxidative stress.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/10/20 alle ore 05:53:15