NMR structure of the pseudo-receiver domain of CikA

Authors

  • Tiyu Gao,

    1. Center for Research on Biological Clocks, Texas A&M University College Station, Texas 77843, USA
    2. Department of Biochemistry & Biophysics, Texas A&M University College Station, Texas 77843, USA
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  • Xiaofan Zhang,

    1. Department of Biochemistry & Biophysics, Texas A&M University College Station, Texas 77843, USA
    2. Department of Biology, Texas A&M University College Station, Texas 77843, USA
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  • Natalia B. Ivleva,

    1. Department of Biochemistry & Biophysics, Texas A&M University College Station, Texas 77843, USA
    2. Department of Biology, Texas A&M University College Station, Texas 77843, USA
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  • Susan S. Golden,

    1. Department of Biochemistry & Biophysics, Texas A&M University College Station, Texas 77843, USA
    2. Department of Biology, Texas A&M University College Station, Texas 77843, USA
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  • Andy LiWang

    Corresponding author
    1. Center for Research on Biological Clocks, Texas A&M University College Station, Texas 77843, USA
    2. Department of Biochemistry & Biophysics, Texas A&M University College Station, Texas 77843, USA
    • Department of Biochemistry & Biophysics, Texas A&M University College Station, TX 77843, USA; fax: (979) 845-9274.
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Abstract

The circadian input kinase (CikA) is a major element of the pathway that provides environmental information to the circadian clock of the cyanobacterium Synechococcus elongatus. CikA is a polypeptide of 754 residues and has three recognizable domains: GAF, histidine protein kinase, and receiver-like. This latter domain of CikA lacks the conserved phospho-accepting aspartyl residue of bona fide receiver domains and is thus a pseudo-receiver (PsR). Recently, it was shown that the PsR domain (1) attenuates the autokinase activity of CikA, (2) is necessary to localize CikA to the cell pole, and (3) is necessary for the destabilization of CikA in the presence of the quinone analog 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone (DBMIB). The solution structure of the PsR domain of CikA, CikAPsR, is presented here. A model of the interaction between the PsR domain and HPK portion of CikA provides a potential explanation for how the PsR domain attenuates the autokinase activity of CikA. Finally, a likely quinone-binding surface on CikAPsR is shown here.

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