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Titolo:
Ultraviolet radiation alters the phosphorylation of RNA polymerase II large subunit and accelerates its proteasome-dependent degradation
Autore:
Luo, ZH; Zheng, JH; Lu, Y; Bregman, DB;
Indirizzi:
Yeshiva Univ Albert Einstein Coll Med, Dept Pathol, Bronx, NY 10461 USA Yeshiva Univ Albert Einstein Coll Med Bronx NY USA 10461 nx, NY 10461 USA Yeshiva Univ Albert Einstein Coll Med, Dept Mol Pharmacol, Bronx, NY 10461USA Yeshiva Univ Albert Einstein Coll Med Bronx NY USA 10461 onx, NY 10461USA
Titolo Testata:
MUTATION RESEARCH-DNA REPAIR
fascicolo: 4, volume: 486, anno: 2001,
pagine: 259 - 274
SICI:
0921-8777(20010904)486:4<259:URATPO>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
CARBOXYL-TERMINAL DOMAIN; TRANSCRIPTION-COUPLED REPAIR; PRE-MESSENGER-RNA; PROTEIN PHOSPHATASE; COCKAYNE-SYNDROME; DNA-DAMAGE; INDUCED UBIQUITINATION; WW DOMAINS; UV; ACTIVATION;
Keywords:
UV response; RNA polymerase II; phosphorylation; proteasome; Cockayne syndrome;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Bregman, DB Yeshiva Univ Albert Einstein Coll Med, Dept Pathol, 1300 Morris Pk Ave, Bronx, NY 10461 USA Yeshiva Univ Albert Einstein Coll Med 1300 Morris Pk Ave Bronx NY USA 10461
Citazione:
Z.H. Luo et al., "Ultraviolet radiation alters the phosphorylation of RNA polymerase II large subunit and accelerates its proteasome-dependent degradation", MUT R-DNA R, 486(4), 2001, pp. 259-274

Abstract

It has been shown that ultraviolet (UV) radiation induces the ubiquitination of the large subunit of RNA polymerase II (RNAP II-LS) as well as its proteasomal degradation. Studies in mammalian cells have indicated that highly phosphorylated forms of RNAP II-LS are preferentially ubiquitinated, but studies in Saccharomyces cerevisiae have provided evidence that unphosphorylated RNAP II-LS is an equally suitable substrate. In the present study, anantibody (ARNA-3) that recognizes all forms of RNAP II-LS, regardless of the phosphorylation status of its C-terminal domain (CTD), was utilized to evaluate the degradation of total cellular RNAP II-LS in human fibroblasts under basal conditions or after UV-C (10 J/m(2)) irradiation. It was found that UV radiation rapidly shifted the phosphorylation profile of RNAP II-LS from a mixture of dephosphorylated and phosphorylated forms to entirely more phosphorylated forms. This shift in phosphorylation status was not blocked by pharmacologic inhibition of either the ERK or p38 pathways, both of which have been implicated in the cellular UV response. In addition to shifting the phosphorylation profile, UV radiation led to net degradation of total RNAP II-LS. UV-induced degradation of RNAP II-LS was also greatly reducedin the presence of the transcriptional and CTD kinase inhibitor DRB. Usinga panel. of protease inhibitors, it was shown that the bulk of UV-induced degradation is proteasome-dependent. However, the UV-induced loss of hypophosphorylated RNAP II-LS was proteasome-independent. Lastly, UV radiation induced a similar shift to all hyperphosphorylated RNAP II-LS in Cockayne syndrome (CS) cells of complementation groups A or B (CSA or CSB) when compared to appropriate controls. The UV-induced degradation rates of RNAP II-LS were not significantly altered when comparing CSA or CSB to repair competentcontrol cells. The implications for the cellular Uv response are discussed. (C) 2001 Elsevier Science B.V All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 03:34:37