Structure of human mitochondrial RNA polymerase elongation complex

Schwinghammer, K.; Cheung, A. C. M.; Morozov, Y. I.; Agaronyan, K.; Temiakov, D.; Cramer, P.

doi:10.1038/nsmb.2683

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Structure of human mitochondrial RNA polymerase elongation complex

MPS-Authors

/persons/resource/persons127020

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

External Resource

http://www.nature.com/nsmb/journal/v20/n11/pdf/nsmb.2683.pdf
(Copyright transfer agreement)

Fulltext (restricted access)

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

Fulltext (public)

1922584.pdf
(Publisher version), 2MB

Supplementary Material (public)

1922584-Suppl-1.pdf
(Supplementary material), 4MB

1922584-Suppl-2.mov
(Supplementary material), 4MB

Citation

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.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0015-3B4E-A

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.