2024-03-19T12:30:52Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/400962021-06-10T12:26:04Zcom_10261_79com_10261_1col_10261_332
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
Nuez, Beatriz
Rojo, Fernando
Salas, Margarita
National Institutes of Health (US)
Ministerio de Economía y Competitividad (España)
Fundación Ramón Areces
Ministerio de Educación y Ciencia (España)
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.
This investigation has been aided by Research Grant SRO1 GM27242-13 from the National Institutes of
Health, by Grant PB90-0091 from Direcci6n General de Investigaci6n Cientfifca y Tecnica, and by an Institutional Grant from Fundaci6n Ram6n Areces. B.N. and F.R. were holders of pre- and
postdoctoral fellowships, respectively, from Ministerio de Educaci6n y Ciencia
Peer reviewed
2011-09-27T10:34:13Z
2011-09-27T10:34:13Z
1992-12-01
artículo
http://purl.org/coar/resource_type/c_6501
Proceedings of the National Academy of Sciences of the USA 89 (23) 11401-11405 (1992)
1091-6490
http://hdl.handle.net/10261/40096
http://dx.doi.org/10.13039/100000002
http://dx.doi.org/10.13039/501100003329
http://dx.doi.org/10.13039/100008054
en
http://www.pnas.org/content/89/23/11401.short
open
National Academy of Sciences (U.S.)