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- W1512662088 abstract "Rpa12p is a subunit of RNA polymerase I formed of two zinc-binding domains. The N-terminal zinc region (positions 1–60) is poorly conserved from yeast to man. The C-terminal domain contains an invariant Q.RSADE..T.F motif shared with the TFIIS elongation factor of RNA polymerase II and its archaeal counterpart. Deletions removing the N-terminal domain fail to grow at 34°C, are sensitive to nucleotide-depleting drugs and become lethal in rpa14-Δ mutants lacking the non-essential RNA polymerase I subunit Rpa14p. They also strongly alter the immunofluorescent properties of RNA polymerase I in the nucleolus. Finally, they prevent the binding of Rpa12p to immunopurified polymerase I and impair a specific two-hybrid interaction with the second largest subunit. In all these respects, N-terminal deletions behave like full deletions. In contrast, C-terminal deletions retaining only the first N-terminal 60 amino acids are indistinguishable from wild type. Thus, the N-terminal zinc domain of Rpa12p determines its anchoring to RNA polymerase I and is the only critical part of that subunit in vivo." @default.
- W1512662088 created "2016-06-24" @default.
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- W1512662088 date "2002-03-22" @default.
- W1512662088 modified "2023-10-16" @default.
- W1512662088 title "Rpa12p, a conserved RNA polymerase I subunit with two functional domains" @default.
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- W1512662088 doi "https://doi.org/10.1046/j.1365-2958.2002.02824.x" @default.
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