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J. Biol. Chem., Vol. 276, Issue 31, 28927-28932, August 3, 2001
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29 Early Promoter C2 by Viral
Protein p6 Is Due to Impairment of Closed Complex*
From the Centro de Biología Molecular "Severo Ochoa"
(Consejo Superior de Investigaciones Científicas-Universidad
Autónoma de Madrid), Universidad Autónoma, Canto
Blanco, 28049 Madrid, Spain
Bacillus subtilis phage 
29 encodes
a very abundant protein, p6, which is a non sequence-specific
DNA-binding protein. Protein p6 has the potential to bind cooperatively
to the phage genome, forming a nucleoprotein complex in which the DNA
adopts a right-handed toroidal conformation winding around a protein
core. The formation of this complex at the right end of the phage
genome where the early promoter C2 is located affects local topology,
which may contribute to the promoter repression, although the
underlying molecular mechanism of this repression is not presently
known. In this study, we analyzed the effect of the p6 nucleoprotein complex on the formation of transcription complexes at the C2 promoter.
The results obtained indicate that the nucleoprotein complex does not
occlude promoter C2 to RNA polymerase because both proteins can bind to
the same DNA molecule. Protein p6 binds along the fragment including
the sequence adjacent to the bound polymerase, altering the structure
of the transcriptional complex and affecting specifically the stability
of the closed complex. The findings presented might help to answer some
of the open questions about the concerted molecular mechanisms of
histone-like proteins as transcriptional silencers.
To whom correspondence should be addressed. Tel.:
34-91-397-8435; Fax: 34-91-397-84-90; E-mail:
msalas@cbm.uam.es.
This article has been cited by other articles:
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V. Gonzalez-Huici, M. Alcorlo, M. Salas, and J. M. Hermoso Phage {phi}29 Proteins p1 and p17 Are Required for Efficient Binding of Architectural Protein p6 to Viral DNA In Vivo J. Bacteriol., December 15, 2004; 186(24): 8401 - 8406. [Abstract] [Full Text] [PDF]
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P. Crucitti, A. M. Abril, and M. Salas Bacteriophage Phi 29 Early Protein p17. SELF-ASSOCIATION AND HETERO-ASSOCIATION WITH THE VIRAL HISTONE-LIKE PROTEIN p6 J. Biol. Chem., February 7, 2003; 278(7): 4906 - 4911. [Abstract] [Full Text] [PDF]
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