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Research Article

Mechanistic Insights Revealed by the Crystal Structure of a Histidine Kinase with Signal Transducer and Sensor Domains

  • Chen Wang equal contributor,

    equal contributor Contributed equally to this work with: Chen Wang, Jiayan Sang

    Affiliations: State Key Laboratory for Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiangan, Xiamen, China, Department of Molecular and Computational Biology, University of Southern California, Los Angeles, California, United States of America

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  • Jiayan Sang equal contributor,

    equal contributor Contributed equally to this work with: Chen Wang, Jiayan Sang

    Affiliation: State Key Laboratory for Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiangan, Xiamen, China

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  • Jiawei Wang,

    Affiliation: Department of Biology and Technology, Tsinghua University, Beijing, China

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  • Mingyan Su,

    Affiliation: State Key Laboratory for Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiangan, Xiamen, China

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  • Jennifer S. Downey,

    Affiliation: Division of Biomedical Science, Herman Ostrow School of Dentistry of University of Southern California, Los Angeles, California, United States of America

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  • Qinggan Wu,

    Affiliation: State Key Laboratory for Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiangan, Xiamen, China

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  • Shida Wang,

    Affiliation: Dental Research Institute, Faculty of Dentistry, University of Toronto, Toronto, Ontario, Canada

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  • Yongfei Cai,

    Affiliation: State Key Laboratory for Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiangan, Xiamen, China

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  • Xiaozheng Xu,

    Affiliation: State Key Laboratory for Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiangan, Xiamen, China

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  • Jun Wu,

    Affiliation: State Key Laboratory for Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiangan, Xiamen, China

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  • Dilani B. Senadheera,

    Affiliation: Dental Research Institute, Faculty of Dentistry, University of Toronto, Toronto, Ontario, Canada

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  • Dennis G. Cvitkovitch,

    Affiliation: Dental Research Institute, Faculty of Dentistry, University of Toronto, Toronto, Ontario, Canada

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  • Lin Chen,

    Affiliation: Department of Molecular and Computational Biology, University of Southern California, Los Angeles, California, United States of America

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  • Steven D. Goodman,

    Affiliation: Division of Biomedical Science, Herman Ostrow School of Dentistry of University of Southern California, Los Angeles, California, United States of America

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  • Aidong Han mail

    ahan@xmu.edu.cn

    Affiliation: State Key Laboratory for Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiangan, Xiamen, China

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  • Published: February 26, 2013
  • DOI: 10.1371/journal.pbio.1001493

Reader Comments (4)

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Light scattering data

Posted by Gastonparis on 05 Mar 2013 at 18:55 GMT

The authors stated that the VicK protein is dimeric in solution. The evidence showed is size exclusion chromatography coupled to a light scattering detector. However, the data showed in figure 1B indicate that the VicK peak is polydisperse. The molecular weight trace (dotted line) goes from 60 to 100 kDa. This result suggest that the VicK protein in solution is in both forms: monomer and dimer, likely, cycling in fast equilibrium between this states.

No competing interests declared.

RE: Light scattering data

ahan replied to Gastonparis on 08 Mar 2013 at 01:28 GMT

This is a valuable comment. Our MALS data do suggest a mixed solution of monomers and dimers of VicK protein prep, however, we have not been able to obtain any other evidence. Only a single species of VicK appears in our native PAGE gel, as shown in supplementary figure 7s. Intriguingly, we failed in purifying heterodimeric VicK even after our intensive efforts. Therefore it is unclear to us whether there is any monomeric VicK in solution.

No competing interests declared.