Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Role of nuclear WW domains and proline-rich proteins in dinoflagellate transcription
Autore:
Guillebault, D; Derelle, E; Bhaud, Y; Moreau, H;
Indirizzi:
Univ Paris 06, CNRS, Lab Arago, Observ Oceanol,UMR 7628, F-66651 Banyuls sur Mer, France Univ Paris 06 Banyuls sur Mer France F-66651 651 Banyuls sur Mer, France
Titolo Testata:
PROTIST
fascicolo: 2, volume: 152, anno: 2001,
pagine: 127 - 138
SICI:
1434-4610(200107)152:2<127:RONWDA>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
RNA-POLYMERASE-II; PROLYL ISOMERASE; TERMINAL DOMAIN; CELL-CYCLE; BINDING; GENE; CHROMOSOMES; EXPRESSION; HUMANS; YEAST;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Moreau, H Univ Paris 06, CNRS, Lab Arago, Observ Oceanol,UMR 7628, BP 44, F-66651 Banyuls sur Mer, France Univ Paris 06 BP 44 Banyuls sur Mer FranceF-66651 Mer, France
Citazione:
D. Guillebault et al., "Role of nuclear WW domains and proline-rich proteins in dinoflagellate transcription", PROTIST, 152(2), 2001, pp. 127-138

Abstract

Dinoflagellates are unique among eukaryotes in their lack of histones and nucleosomes, and permanently condensed chromosomes. These unusual features raise questions as how chromatin condensation and gene expression are achieved. In this study, we investigated nuclear proteins potentially implicatedin the regulation of the transcription. Dinap1 is a dinoflagellate nuclearprotein that has a WW domain and is synthesized mainly in G1 and S phases of the cell cycle. In this study, we found that Dip1, a proline-rich potential ligand of Dinap1, and DapC, a Dip1 potential ligand, were both present in the nucleus of Crypthecodinium cohnii during the G1 phase. Dip1 contained a PPXY motif, and its domain organization was similar to that of the splicing factor FBP21 in that it possessed one zinc finger and two WW domains. Although DapC has no known homolog, 22 repeats of a PPXPXGX heptapeptide were identified at the N-terminus, and this structure is similar to that of the C-terminal part of the mouse splicing factor SAP62. Dinap1 was co-precipitated with Dip1 and DapC in vitro and in vivo, but despite their nuclear location, these three proteins did not bind directly to DNA. Dinap1 activated up to 40% of the basal transcription activity of C. cohnii in an in vitro assay, whereas DapC inhibited it by 40% and Dip1 had no effect. These dinoflagellate proteins appear to be the subunits of a nuclear complex that may be involved in regulating transcription.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 12:49:00