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Rpa43 and its partners in the yeast RNA polymerase I transcription complex

Rpa43 and its partners in the yeast RNA polymerase I transcription complex,10.1016/j.febslet.2011.09.011,Febs Letters,Frédéric Beckouët,Sylvie Mariott

Rpa43 and its partners in the yeast RNA polymerase I transcription complex   (Citations: 1)
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An Rpa43/Rpa14 stalk protrudes from RNA polymerase I (RNAPI), with homology to Rpb7/Rpb4 (RNAPII), Rpc25/Rpc17 (RNAPIII) and RpoE/RpoF (archaea). In fungi and vertebrates, Rpa43 contains hydrophilic domains forming about half of its size, but these domains lack in Schizosaccharomyces pombe and most other eukaryote lineages. In Saccharomyces cerevisiae, they can be lost with little or no growth effect, as shown by deletion mapping and by domain swapping with fission yeast, but genetically interact with rpa12Δ, rpa34Δ or rpa49Δ, lacking non-essential subunits important for transcript elongation. Two-hybrid data and other genetic evidence suggest that Rpa43 directly bind Spt5, an RNAPI elongation factor also acting in RNAPII-dependent transcription, and may also interact with the nucleosomal chaperone Spt6.
Journal: Febs Letters - FEBS LETT , vol. 585, no. 21, pp. 3355-3359, 2011
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