Structure of human mitochondrial RNA polymerase

Rieke Ringel, Marina Sologub, Yaroslav I. Morozov, Dmitry Litonin, Patrick Cramer () and Dmitry Temiakov ()
Additional contact information
Rieke Ringel: Center for Integrated Protein Science Munich (CIPSM), Ludwig-Maximilians-Universität München, Feodor-Lynen-Strasse 25
Marina Sologub: University of Medicine and Dentistry of New Jersey, School of Osteopathic Medicine, 2 Medical Center Dr
Yaroslav I. Morozov: University of Medicine and Dentistry of New Jersey, School of Osteopathic Medicine, 2 Medical Center Dr
Dmitry Litonin: Center for Integrated Protein Science Munich (CIPSM), Ludwig-Maximilians-Universität München, Feodor-Lynen-Strasse 25
Patrick Cramer: Center for Integrated Protein Science Munich (CIPSM), Ludwig-Maximilians-Universität München, Feodor-Lynen-Strasse 25
Dmitry Temiakov: University of Medicine and Dentistry of New Jersey, School of Osteopathic Medicine, 2 Medical Center Dr

Nature, 2011, vol. 478, issue 7368, 269-273

Abstract: A mitochondrial polymerase The transcription of the mitochondrial genome is carried out by a single-subunit RNA polymerase (mtRNAP), which is distantly related to the RNAP of bacteriophage T7. Unlike T7 RNAP, the mtRNAP requires additional transcription factors (TFAM and TFB2M) for transcription initiation. The crystal structure of human mtRNAP has now been determined, revealing novel domains and mechanistic adaptations that explain the requirement for TFAM and TFB2M. These findings provide insights into the evolution of polymerases from simple self-sufficient enzymes to large multi-subunit complexes.

Date: 2011
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DOI: 10.1038/nature10435

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