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If pol i is −1, then the polarity of the data is inverted.
DNA unwinding between the Pol I protrusion and clamp domains enables cleft contraction, resulting in an active Pol I conformation and RNA synthesis.
RNA polymerase I (Pol I) is a 14-subunit enzyme that solely synthesizes pre-ribosomal RNA.
Importantly, these data present a mechanistic basis for the requirement of A12.2 in Pol I termination.
Recently, the crystal structure of apo Pol I gave unprecedented insight into its molecular architecture.
Here, we present three cryo-EM structures of elongating Pol I, two at 4.0 Å and one at 4.6 Å resolution, and a Pol I open complex at 3.8 Å resolution.
Similar(6)
NM1 has therefore been proposed to connect Pol I with the rDNA through direct interactions with the Pol I-associated actin and chromatin, respectively.
Collectively, our data suggest a role for Pol I-associated FACT, as a histone chaperone, in passage of Pol I through chromatin templates in cells.
RNA Pol I transcription requires the SL1 complex, which is composed of the TBP and three Pol I-specific TAFs, TAFI110, TAFI63 and TAFI48.
Yet evidence linking FACT to Pol I-dependent transcription in cells was missing.
Transcription in eukaryotes is performed by three different RNA Polymerases, Pol I-III.
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