PMID: 9192631Jun 24, 1997Paper

Activation of RNA polymerase II by topologically linked DNA-tracking proteins

Proceedings of the National Academy of Sciences of the United States of America
M OuhammouchE P Geiduschek

Abstract

Almost all proteins mediating transcriptional activation from promoter-distal sites attach themselves, directly or indirectly, to specific DNA sequence elements. Nevertheless, a single instance of activation by a prokaryotic topologically linked DNA-tracking protein has also been demonstrated. The scope of the latter class of transcriptional activators is broadened in this work. Heterologous fusion proteins linking the transcriptional activation domain of herpes simplex virus VP16 protein to the sliding clamp protein beta of the Escherichia coli DNA polymerase III holoenzyme are shown to function as topologically DNA-linked activators of yeast and Drosophila RNA polymerase II. The beta:VP16 fusion proteins must be loaded onto DNA by the clamp-loading E. coli gamma complex to be transcriptionally active, but they do not occupy fixed sites on the DNA. The DNA-loading sites of these activators have all the properties of enhancers: they can be inverted and their locations relative to the transcriptional start site are freely adjustable.

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Citations

Jun 6, 2009·Annual Review of Biochemistry·E Peter Geiduschek
Oct 30, 2010·Virology Journal·E Peter Geiduschek, George A Kassavetis
Jul 22, 1998·Proceedings of the National Academy of Sciences of the United States of America·W K VersawE H Bresnick
Mar 13, 1998·Chemistry & Biology·K Ryan, E T Kool
Feb 20, 2021·Nature Communications·Jing ShiYu Feng

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