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A primase subunit essential for efficient primer synthesis by an archaeal eukaryotic-type primase

Author

Listed:
  • Bing Liu

    (State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences)

  • Songying Ouyang

    (National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences)

  • Kira S. Makarova

    (National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health)

  • Qiu Xia

    (State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences)

  • Yanping Zhu

    (National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences)

  • Zhimeng Li

    (State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences)

  • Li Guo

    (State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences)

  • Eugene V. Koonin

    (National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health)

  • Zhi-Jie Liu

    (National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences)

  • Li Huang

    (State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences)

Abstract

Archaea encode a eukaryotic-type primase comprising a catalytic subunit (PriS) and a noncatalytic subunit (PriL). Here we report the identification of a primase noncatalytic subunit, denoted PriX, from the hyperthermophilic archaeon Sulfolobus solfataricus. Like PriL, PriX is essential for the survival of the organism. The crystallographic analysis complemented by sensitive sequence comparisons shows that PriX is a diverged homologue of the C-terminal domain of PriL but lacks the iron–sulfur cluster. Phylogenomic analysis provides clues on the origin and evolution of PriX. PriX, PriL and PriS form a stable heterotrimer (PriSLX). Both PriSX and PriSLX show far greater affinity for nucleotide substrates and are substantially more active in primer synthesis than the PriSL heterodimer. In addition, PriL, but not PriX, facilitates primer extension by PriS. We propose that the catalytic activity of PriS is modulated through concerted interactions with the two noncatalytic subunits in primer synthesis.

Suggested Citation

  • Bing Liu & Songying Ouyang & Kira S. Makarova & Qiu Xia & Yanping Zhu & Zhimeng Li & Li Guo & Eugene V. Koonin & Zhi-Jie Liu & Li Huang, 2015. "A primase subunit essential for efficient primer synthesis by an archaeal eukaryotic-type primase," Nature Communications, Nature, vol. 6(1), pages 1-11, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8300
    DOI: 10.1038/ncomms8300
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