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  The archaeal RNA polymerase subunit P and the eukaryotic polymerase subunit Rpb12 are interchangeable in vivo and in vitro.

Reich, C., Zeller, M., Milkereit, P., Hausner, W., Cramer, P., Tschochner, H., et al. (2009). The archaeal RNA polymerase subunit P and the eukaryotic polymerase subunit Rpb12 are interchangeable in vivo and in vitro. Molecular Microbiology, 71(4), 989-1002.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-7B7A-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-C529-4
Genre: Journal Article

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 Creators:
Reich, C., Author
Zeller, M., Author
Milkereit, P., Author
Hausner, W., Author
Cramer, P.1, Author              
Tschochner, H., Author
Thomm, M., Author
Affiliations:
1Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

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 Abstract: The general subunit of all three eukaryotic RNA polymerases, Rpb12, and subunit P of the archaeal enzyme show sequence similarities in their N-terminal zinc ribbon and some highly conserved residues in the C-terminus. We report here that archaeal subunit P under the control of a strong yeast promoter could complement the lethal phenotype of a RPB12 deletion mutant and that subunit Rpb12 from yeast can functionally replace subunit P during reconstitution of the archaeal RNA polymerase. The ΔP enzyme is unable to form stable open complexes, but can efficiently extend a dinucleotide on a premelted template or RNA on an elongation scaffold. This suggests that subunit P is directly or indirectly involved in promoter opening. The activity of the ΔP enzyme can be rescued by the addition of Rpb12 or subunit P to transcription reactions. Mutation of cysteine residues in the zinc ribbon impair the activity of the enzyme in several assays and this mutated form of P is rapidly replaced by wild-type P in transcription reactions. The conserved zinc ribbon in the N-terminus seems to be important for proper interaction of the complete subunit with other RNA polymerase subunits and a 17-amino-acid C-terminal peptide is sufficient to support all basic RNA polymerase functions in vitro.

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Language(s): eng - English
 Dates: 2008-12-182009-02
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: CoNE: 1111/j.1365-2958.2008.06577.x
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Title: Molecular Microbiology
Source Genre: Journal
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Pages: - Volume / Issue: 71 (4) Sequence Number: - Start / End Page: 989 - 1002 Identifier: -