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Título: | Alternative mechanisms of transcriptional activation by Rap1p |
Autor: | Idrissi, Fátima-Zahra CSIC; García-Reyero, Natàlia; Fernández-Larrea, Juan B.; Piña, Benjamín CSIC ORCID | Fecha de publicación: | 17-may-2001 | Editor: | American Society for Biochemistry and Molecular Biology | Citación: | Journal of Biological Chemistry 276(28): 26090-26098 (2001) | Resumen: | Single Rap1p DNA-binding sites are poor activators of transcription of yeast minimal promoters, even when fully occupied in vivo. This low efficiency is due to two independent repression mechanisms as follows: one that requires the presence of histones, and one that requires Hrs1p, a component of the RNA polymerase II mediator complex. Both repression mechanisms were greatly reduced for constructs with tandemly arranged sites. In these constructs, UASrpg sequences (ACACCCATACATTT) activated better than telomere-like sequences (ACACCCACACACCC) in an orientation-dependent manner. Both mutations in the SWI/SNF complex and a deletion of amino acids 597--629 of Rap1p (Tox domain) decreased synergistic effects of contiguous telomeric sites. Conversely, deletion of amino acids 700--798 of Rap1p (Sil domain) made UASrpg and telomeric sites functionally indistinguishable. We propose that the Sil domain masks the main transactivation domain of Rap1p in Rap1p-telomere complexes, where the Tox domain behaves as a secondary activation domain, probably by interacting with chromatin-remodeling complexes. Rap1p DNA-binding sites in ribosomal protein gene promoters are mainly UASrpg-like; their replacement by telomeric sequences in one of these promoters (RPS17B) decreased transcription by two-thirds. The functional differences between UASrpgs and telomeric sequences may thus contribute to the differential expression of Rap1p-regulated promoters in vivo. | Descripción: | 9 pages, 6 figures, 3 tables.-- PMID: 11358963 [PubMed].-- Printed version published Jul 13, 2001. | Versión del editor: | http://dx.doi.org/10.1074/jbc.M101746200 | URI: | http://hdl.handle.net/10261/27469 | DOI: | 10.1074/jbc.M101746200 | ISSN: | 0021-9258 | E-ISSN: | 1083-351X |
Aparece en las colecciones: | (IDAEA) Artículos |
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