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An alternative RNA polymerase I structure reveals a dimer hinge

Title data

Kostrewa, Dirk ; Kuhn, Claus-D. ; Engelhard, Christoph ; Cramer, Patrick:
An alternative RNA polymerase I structure reveals a dimer hinge.
In: Acta Crystallographica Section D. Vol. 71 (September 2015) Issue 9 . - pp. 1850-1855.
ISSN 1399-0047
DOI: https://doi.org/10.1107/S1399004715012651

Abstract in another language

RNA polymerase I (Pol I) is the central, 14-subunit enzyme that synthesizes the ribosomal RNA (rRNA) precursor in eukaryotic cells. The recent crystal structure of Pol I at 2.8 Å resolution revealed two novel elements: the `expander' in the active-centre cleft and the `connector' that mediates Pol I dimerization [Engel et al. (2013), Nature (London), 502, 650-655]. Here, a Pol I structure in an alternative crystal form that was solved by molecular replacement using the original atomic Pol I structure is reported. The resulting alternative structure lacks the expander but still shows an expanded active-centre cleft. The neighbouring Pol I monomers form a homodimer with a relative orientation distinct from that observed previously, establishing the connector as a hinge between Pol I monomers.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences
Profile Fields > Advanced Fields > Molecular Biosciences
Research Institutions > Research Centres > Bayreuth Center for Molecular Biosciences - BZMB
Profile Fields
Profile Fields > Advanced Fields
Research Institutions
Research Institutions > Research Centres
Result of work at the UBT: No
DDC Subjects: 500 Science > 570 Life sciences, biology
Date Deposited: 10 Jan 2017 10:45
Last Modified: 10 Jan 2017 10:45
URI: https://eref.uni-bayreuth.de/id/eprint/35631