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  Structure of human mitochondrial RNA polymerase elongation complex

Schwinghammer, K., Cheung, A. C. M., Morozov, Y. I., Agaronyan, K., Temiakov, D., & Cramer, P. (2013). Structure of human mitochondrial RNA polymerase elongation complex. Nature Structural and Molecular Biology, 20(11), 1298-1303. doi:10.1038/nsmb.2683.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-3B4E-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-48F4-C
Genre: Journal Article

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 Creators:
Schwinghammer, K., Author
Cheung, A. C. M., Author
Morozov, Y. I., Author
Agaronyan, K., Author
Temiakov, D., Author
Cramer, P.1, Author              
Affiliations:
1Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

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 Abstract: Here we report the crystal structure of the human mitochondrial RNA polymerase (mtRNAP) transcription elongation complex, determined at 2.65-Å resolution. The structure reveals a 9-bp hybrid formed between the DNA template and the RNA transcript and one turn of DNA both upstream and downstream of the hybrid. Comparisons with the distantly related RNA polymerase (RNAP) from bacteriophage T7 indicates conserved mechanisms for substrate binding and nucleotide incorporation but also strong mechanistic differences. Whereas T7 RNAP refolds during the transition from initiation to elongation, mtRNAP adopts an intermediary conformation that is capable of elongation without refolding. The intercalating hairpin that melts DNA during T7 RNAP initiation separates RNA from DNA during mtRNAP elongation. Newly synthesized RNA exits toward the pentatricopeptide repeat (PPR) domain, a unique feature of mtRNAP with conserved RNA-recognition motifs.

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Language(s): eng - English
 Dates: 2013-10-06
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/nsmb.2683
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Title: Nature Structural and Molecular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 20 (11) Sequence Number: - Start / End Page: 1298 - 1303 Identifier: -