In bacteriophage lambda, the expression of delayed-early genes is regulated by the lambda N protein through formation of a ribonucleoprotein complex that allows RNA polymerase to read through termination sites.  This antitermination complex consists of the N-utilization (nut) site-coded RNA (boxA and boxB) of the naqscent RNA transcript, N protein, host factors (NusA, NusB, S10, and NusG), and RNA polymerase.  Using a bacterial reporter assay, we have also shown that the core N peptide-boxB RNA interaction can be replaced by heterologous interactions such as those between the HIV Rev peptide-RRE RNA (Harada, K. et al., Nature, 1996).  However, relatively small changes in the spatial orientation of the RNA sitehave been shown to result in large changes in antitermination activity (Horiya, S. et al., Mol. Microbiol., 2009).  Here, we show how antitermination activity can be manipulated in a predictable manner by engineering the spatial orientation of the core RNA-peptide complex.

Engineering the spatial orientation of a core RNA-peptide interaction within a functional ribonucleoprotein complex

243rd National Meeting (2012)

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