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The X-ray crystal structure of RNA polymerase from Archaea

Author

Listed:
  • Akira Hirata

    (The Pennsylvania State University, University Park, Pennsylvania 16802, USA)

  • Brianna J. Klein

    (The Pennsylvania State University, University Park, Pennsylvania 16802, USA)

  • Katsuhiko S. Murakami

    (The Pennsylvania State University, University Park, Pennsylvania 16802, USA)

Abstract

Three RNAPs is company The Archaea were once thought of as the more primitive of the two prokaryotic lineages, but they are now considered to be more closely related to the eukaryotes (or Eukarya) than to the Bacteria. Determination of the crystal structure of archaeal RNA polymerase (RNAP) now allows a structural comparison of the transcription machinery between all three domains of life. The archaeal enzyme shows striking structural similarities to the eukaryotic equivalent, and should be a useful model system for the dissection of the molecular basis of eukaryote transcription.

Suggested Citation

  • Akira Hirata & Brianna J. Klein & Katsuhiko S. Murakami, 2008. "The X-ray crystal structure of RNA polymerase from Archaea," Nature, Nature, vol. 451(7180), pages 851-854, February.
    • Handle: RePEc:nat:nature:v:451:y:2008:i:7180:d:10.1038_nature06530
    DOI: 10.1038/nature06530
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    Cited by:

    1. Guoliang Zhu & Fei Xi & Wuxia Zeng & Yifei Zhao & Weijun Cao & Chen Liu & Fan Yang & Yi Ru & Shuqi Xiao & Shilei Zhang & Huanan Liu & Hong Tian & Fayu Yang & Biao Lu & Shukai Sun & Haiyang Song & Bozh, 2025. "Structural basis of RNA polymerase complexes in African swine fever virus," Nature Communications, Nature, vol. 16(1), pages 1-13, December.

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