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Structural basis of HutP-mediated anti-termination and roles of the Mg2+ ion and L-histidine ligand

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  • Thirumananseri Kumarevel

    (Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology (AIST))

  • Hiroshi Mizuno

    (National Institute of Agrobiological Sciences
    NEC Soft. Ltd)

  • Penmetcha K. R. Kumar

    (Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology (AIST))

Abstract

HutP regulates the expression of the hut structural genes of Bacillus subtilis by an anti-termination mechanism and requires two components, Mg2+ ions and l-histidine. HutP recognizes three UAG triplet units, separated by four non-conserved nucleotides on the terminator region. Here we report the 1.60-Å resolution crystal structure of the quaternary complex (HutP–l-histidine–Mg2+–21-base single-stranded RNA). In the complex, the RNA adopts a novel triangular fold on the hexameric surface of HutP, without any base-pairing, and binds to the protein mostly by specific protein–base interactions. The structure explains how the HutP and RNA interactions are regulated critically by the l-histidine and Mg2+ ion through the structural rearrangement. To gain insights into these structural rearrangements, we solved two additional crystal structures (uncomplexed HutP and HutP–l-histidine–Mg2+) that revealed the intermediate structures of HutP (before forming an active structure) and the importance of the Mg2+ ion interactions in the complexes.

Suggested Citation

  • Thirumananseri Kumarevel & Hiroshi Mizuno & Penmetcha K. R. Kumar, 2005. "Structural basis of HutP-mediated anti-termination and roles of the Mg2+ ion and L-histidine ligand," Nature, Nature, vol. 434(7030), pages 183-191, March.
    • Handle: RePEc:nat:nature:v:434:y:2005:i:7030:d:10.1038_nature03355
    DOI: 10.1038/nature03355
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