title: Molecular interactions and protein-induced DNA hairpin in the transcriptional control of bacteriophage ø29 DNA.
abstract: Studies on the regulation of phage Ø29 gene expression revealed a new mechanism to accomplish simultaneous activation and repression of transcription leading to orderly gene expression. Two phage-encoded early proteins, p4 and p6, bind synergistically to DNA, modifying the topology of the sequences encompassing early promoters A2c and A2b and late promoter A3 in a hairpin that allows the switch from early to late transcription. Protein p6 is a nucleoid-like protein that binds DNA in a non-sequence specific manner. Protein p4 is a sequence-specific DNA binding protein with multifaceted sequence-readout properties. The protein recognizes the chemical signature of only one DNA base on the inverted repeat of its target sequence through a direct-readout mechanism. In addition, p4 specific binding depends on the recognition of three A-tracts by indirect-readout mechanisms. The biological importance of those three A-tracts resides in their individual properties rather than in the global curvature that they may induce.
authors: Institute Eladio Viñuela (CSIC), Center of Molecular Biology Severo Ochoa (CSIC-UAM), Madrid Autonomous University, 28049 Madrid, Spain; E-Mail: msalas@cbm.uam.es.
authors: Ana
authors: A
authors: Camacho
authors: Margarita
authors: M
authors: Salas
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