Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Herpes simplex virus 1 alpha regulatory protein ICP0 functionally interacts with cellular transcription factor BMAL1
Autore:
Kawaguchi, Y; Tanaka, M; Yokoymama, A; Matsuda, G; Kato, K; Kagawa, H; Hirai, K; Roizman, B;
Indirizzi:
Univ Chicago, Marjorie B Kovler Viral Oncol Labs, Chicago, IL 60637 USA Univ Chicago Chicago IL USA 60637 Viral Oncol Labs, Chicago, IL 60637 USA Tokyo Med & Dent Univ, Med Res Inst, Div Virol & Immunol, Dept Tumor Virol, Tokyo 1138510, Japan Tokyo Med & Dent Univ Tokyo Japan 1138510 or Virol, Tokyo 1138510, Japan Promega KK, Chuo Ku, Tokyo 1030004, Japan Promega KK Tokyo Japan 1030004Promega KK, Chuo Ku, Tokyo 1030004, Japan
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 4, volume: 98, anno: 2001,
pagine: 1877 - 1882
SICI:
0027-8424(20010213)98:4<1877:HSV1AR>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELONGATION-FACTOR 1-DELTA; AH-RECEPTOR; KINASE; GENE; PAS; DOMAIN; MATURATION; MECHANISM; COMPLEXES; CLONING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Roizman, B Univ Chicago, Marjorie B Kovler Viral Oncol Labs, 910 E 58th St, Chicago, IL 60637 USA Univ Chicago 910 E 58th St Chicago IL USA 60637 o, IL 60637 USA
Citazione:
Y. Kawaguchi et al., "Herpes simplex virus 1 alpha regulatory protein ICP0 functionally interacts with cellular transcription factor BMAL1", P NAS US, 98(4), 2001, pp. 1877-1882

Abstract

The infected cell protein no. 0 (ICP0) of herpes simplex virus 1 (HSV-1) is a promiscuous transactivator shown to enhance the expression of gene introduced into cells by infection or transfection, At the molecular level, ICP0 is a 775-aa ring finger protein localized initially in the nucleus and late in infection in the cytoplasm and mediates the degradation of several proteins and stabilization of others. None of the known functions at the molecular level account for the apparent activity of ICP0 as a transactivator, Here we report that ICP0 functionally interacts with cellular transcriptionfactor BMAL1, a member of the basic helix-loop-helix PER-ARNT-SIM (PAS) super family of transcriptional regulators. Specifically, sequences mapped tothe exon II of ICP0 interacted with BMAL1 in the yeast two-hybrid system and in reciprocal pull-down experiments in vitro. Moreover, the enhancement of transcription of a luciferase reporter construct whose promoter contained multiple BMAL1-binding sites by ICP0 and BMAL1 was significantly greater than that observed by ICP0 or BMAL1 alone. Although the level of BMAL1 present in nuclei of infected cells remained unchanged between 3 and 8 h after infection, the level of cytoplasmic BMAL1 was reduced at 8 h after infection. The reduction of cytoplasmic BMAL1 was significantly greater in cells infected with the ICP0-null mutant than in the wild-type virus-infected cells, suggesting that ICP0 mediates partial stabilization of the protein. Theseresults indicate that ICP0 interacts physically and functionally with at least one cellular transcription-regulatory factor.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/08/20 alle ore 10:03:09