An alternative RNA polymerase I structure reveals a dimer hinge.

Kostrewa, D.; Kuhn, C. D.; Engel, C.; Cramer, P.

doi:10.1107/S1399004715012651

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

An alternative RNA polymerase I structure reveals a dimer hinge.

MPS-Authors

/persons/resource/persons172942

Engel, C.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons127020

Cramer, P.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

External Resource

http://journals.iucr.org/d/issues/2015/09/00/mn5095/index.html
(Publisher version)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Kostrewa, D., Kuhn, C. D., Engel, C., & Cramer, P. (2015). An alternative RNA polymerase I structure reveals a dimer hinge. Acta Crystallographica D, 71(9), 1850-1855. doi:10.1107/S1399004715012651.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0028-4C99-5

Abstract

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.