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  An alternative RNA polymerase I structure reveals a dimer hinge.

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-4C99-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-DC81-0
Genre: Journal Article

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2186309.pdf (Publisher version), 3MB
 
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 Creators:
Kostrewa, D., Author
Kuhn, C. D., Author
Engel, C.1, Author              
Cramer, P.1, Author              
Affiliations:
1Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

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Free keywords: RNA polymerase I; dimer; hinge; connector
 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.

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Language(s): eng - English
 Dates: 2015-08-25
 Publication Status: Published online
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1107/S1399004715012651
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Title: Acta Crystallographica D
Source Genre: Journal
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Pages: - Volume / Issue: 71 (9) Sequence Number: - Start / End Page: 1850 - 1855 Identifier: -