7AOC
Schizosaccharomyces pombe RNA polymerase I (monomer)
Summary for 7AOC
Entry DOI | 10.2210/pdb7aoc/pdb |
EMDB information | 11840 |
Descriptor | DNA-directed RNA polymerase I subunit rpa1, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerases I and III subunit RPAC2, ... (13 entities in total) |
Functional Keywords | transcription |
Biological source | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) More |
Total number of polymer chains | 12 |
Total formula weight | 493737.18 |
Authors | Heiss, F.,Daiss, J.,Becker, P.,Engel, C. (deposition date: 2020-10-14, release date: 2021-02-24, Last modification date: 2024-10-16) |
Primary citation | Heiss, F.B.,Daiss, J.L.,Becker, P.,Engel, C. Conserved strategies of RNA polymerase I hibernation and activation. Nat Commun, 12:758-758, 2021 Cited by PubMed Abstract: RNA polymerase (Pol) I transcribes the ribosomal RNA precursor in all eukaryotes. The mechanisms 'activation by cleft contraction' and 'hibernation by dimerization' are unique to the regulation of this enzyme, but structure-function analysis is limited to baker's yeast. To understand whether regulation by such strategies is specific to this model organism or conserved among species, we solve three cryo-EM structures of Pol I from Schizosaccharomyces pombe in different functional states. Comparative analysis of structural models derived from high-resolution reconstructions shows that activation is accomplished by a conserved contraction of the active center cleft. In contrast to current beliefs, we find that dimerization of the S. pombe polymerase is also possible. This dimerization is achieved independent of the 'connector' domain but relies on two previously undescribed interfaces. Our analyses highlight the divergent nature of Pol I transcription systems from their counterparts and suggest conservation of regulatory mechanisms among organisms. PubMed: 33536435DOI: 10.1038/s41467-021-21031-8 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.84 Å) |
Structure validation
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