Reference: Beckouet F, et al. (2008) Two RNA Polymerase I Subunits Control the Binding and Release of Rrn3 during Transcription. Mol Cell Biol 28(5):1596-1605

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Abstract

Rpa34 and Rpa49 are non-essential subunits of RNA polymerase I, conserved from yeast to man. Rpa34 binds an N-terminal region of Rpa49 in a two-hybrid assay and is lost from RNA polymerase in an rpa49 mutant lacking this Rpa34-binding domain, whereas rpa34Delta weakens the binding of Rpa49 to RNA polymerase. rpa34Delta is caffeine-sensitive and is lethal in top1Delta and in rpa14Delta, rpa135-L656P and rpa135-D398N RNA polymerase mutants. These defects are shared with rpa49Delta and suppressed by over-expressing Rpa49, and are thus presumably mediated by Rpa49 itself. rpa49 mutants lacking the Rpa34-binding domain essentially behave like rpa34Delta, but rpa49Delta and rpa49-338::HIS3 (lacking the conserved C-end of Rpa49) reduce polymerase occupancy at 30 degrees C, fail to grow at 25 degrees C and are sensitive to 6-azauracil and mycophenolate. Mycophenolate almost fully dissociates the mutant polymerase from its rDNA template. These mutants have a dual effect on the Rrn3/TIF-IA factor. They partly impair its recruitment to the rDNA promoter, which is bypassed by rpa43-35,326, an N-terminal deletion of the Rpa43 subunit, and strongly reduce the release of the Rrn3 initiation factor during elongation. These data suggest a dual role of the Rpa49-Rpa34 dimer during the recruitment of Rrn3 and its subsequent dissociation from the elongating polymerase.

Reference Type
Journal Article
Authors
Beckouet F, Labarre-Mariotte S, Albert B, Imazawa Y, Werner M, Gadal O, Nogi Y, Thuriaux P
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