Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/40096
Title: Phage phi 29 regulatory protein p4 stabilizes the binding of the RNA polymerase to the late promoter in a process involving direct protein-protein contacts
Authors: Nuez, B., Rojo, Fernando, Salas, Margarita
Issue Date: 1-Dec-1992
Publisher: National Academy of Sciences (U.S.)
Abstract: Transcription from the late promoter, PA3, of Bacillus subtilis phage phi 29 is activated by the viral regulatory protein p4. A kinetic analysis of the activation process has revealed that the role of protein p4 is to stabilize the binding of RNA polymerase to the promoter as a closed complex without significantly affecting further steps of the initiation process. Electrophoretic band-shift assays performed with a DNA fragment spanning only the protein p4 binding site showed that RNA polymerase could efficiently retard the complex formed by protein p4 bound to the DNA. Similarly, when a DNA fragment containing only the RNA polymerase-binding region of PA3 was used, p4 greatly stimulated the binding of RNA polymerase to the DNA. These results strongly suggest that p4 and RNA polymerase contact each other at the PA3 promoter. In the light of current knowledge of the p4 activation mechanism, we propose that direct contacts between the two proteins participate in the activation process.
Publisher version (URL): http://www.pnas.org/content/89/23/11401.short
URI: http://hdl.handle.net/10261/40096
ISSN: 1091-6490
Citation: Proceedings of the National Academy of Sciences of the USA 89 (23) 11401-11405 (1992)
Appears in Collections:(CBM) Artículos

Files in This Item:
File Description SizeFormat 
PNAS-1992-Nuez-11401-5.pdf1,41 MBAdobe PDFView/Open
Show full item record
 
CSIC SFX LinksSFX Query

Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.