Regularities in the E. coli promoters composition in connection with the DNA strands interaction and promoter activity
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The energy of interaction between DNA strands in promoters is of great functional importance. Visualization of the energy of DNA strands distribution in promoter sequences was achieved. The separation of promoters in groups by their energetic properties enables evaluation of the dependence of promoter strength on the energetic properties. The analysis of groups (clusters) of promoters distributed by the energy of DNA strands interaction in −55, −35, −10 and +6 sequences indicates their connection with the transcriptional activity.
Key wordsDNA sequence Promoter strength DNA chains interaction energy DNA sequences classification
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- Craig, M.L., Tsodikov, O.V., McQuade, K.L., Schlax, P.E.Jr, Capp, M.W., Saecker, R.M., Record, M.T.Jr., 1998. DNA footprints of the two kinetically significant intermediates in formation of an RNA polymerase-promoter open complex: evidence that interactions with start site and downstream DNA induce sequential conformational changes in polymerase and DNA. J. Mol. Biol., 283(4): 741–756. [doi:10.1006/jmbi.1998.2129]PubMedCrossRefGoogle Scholar
- Lewin, B., 2004. Genes-VIII. Pearson Prenice Hall, New York.Google Scholar
- Record, M.T.Jr, Reznikoff, W.S., Craig, M.L., McQuade, K.L., Schlaz, P.J., 1996. Escherichia coli RNA Polymerase (Eσ70), Promoters, and the Kinetics of the Steps of Transcription Initiation. In: Neidhardt, F.C., Curtiss III, R., Ingraham, J.L., Lin, E.C.C., Low, K.R., Magasanik, B., Reznikoff, W.S., Riley, M., Schaechter, M., Umbarger, H.E. (Eds.), Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. ASM Press, Washington DC, p.792–820.Google Scholar
- Saecker, R.M., Tsodikov, O.V., McQuade, K.L., Schlax, P.E.Jr, Capp, M.W., Record, M.T.Jr, 2002. Kinetic studies and structural models of the association of E. coli sigma (70) RNA polymerase with the lambdaP (R) promoter: large scale conformational changes in forming the kinetically significant intermediates. J. Mol. Biol., 319(3):649–671. [doi:10.1016/S0022-2836(02)00293-0]PubMedCrossRefGoogle Scholar