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- W2080648295 endingPage "1921" @default.
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- W2080648295 abstract "In eukaryotes the genetic material is contained within a coiled, protein-coated structure known as chromatin. RNA polymerases must recognize specific nucleoprotein assemblies and maintain contact with the underlying DNA duplex for many thousands of base pairs. Template-bound lac operon repressor from Escherichia coli arrests RNA polymerase II in vitro and in vivo [Kuhn, A., Bartsch, I. & Grummt, I. (1990) Nature (London) 344, 559-562; Deuschele, U., Hipskind, R. A. & Bujard, H. (1990) Science 248, 480-483]. We show that in a reconstituted transcription system, elongation factor SII enables RNA polymerase II to proceed through this blockage at high efficiency. lac repressor-arrested elongation complexes display an SII-activated transcript cleavage reaction, an activity associated with transcriptional read-through of a previously characterized region of bent DNA. This demonstrates factor-dependent transcription by RNA polymerase II through a sequence-specific DNA-binding protein. Nascent transcript cleavage may be a general mechanism by which RNA polymerase II can bypass many transcriptional impediments." @default.
- W2080648295 created "2016-06-24" @default.
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- W2080648295 date "1993-03-01" @default.
- W2080648295 modified "2023-09-27" @default.
- W2080648295 title "Elongation factor SII-dependent transcription by RNA polymerase II through a sequence-specific DNA-binding protein." @default.
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- W2080648295 doi "https://doi.org/10.1073/pnas.90.5.1917" @default.
- W2080648295 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/45991" @default.
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