Purification of recombinant Chlamydia trachomatis histone H1-like protein Hc2, and comparative functional analysis of Hc2 and Hc1

Authors

  • Lotte Bang Pedersen,

    1. Department of Medical Microbiology and Immunology, Bartholin Building, University of Aarhus, DK-8000 Aarhus C. Denmark.
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  • Svend Birkelund,

    1. Department of Medical Microbiology and Immunology, Bartholin Building, University of Aarhus, DK-8000 Aarhus C. Denmark.
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  • Gunna Christiansen

    Corresponding author
    1. Department of Medical Microbiology and Immunology, Bartholin Building, University of Aarhus, DK-8000 Aarhus C. Denmark.
    • *For correspondence. Tel. 89421749; Fax 86196128.

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Summary

The metabolically inactive developmental form of Chlamydia trachomatis, the elementary body, contains two very basic DNA-binding proteins with homology to eukaryotic histone H1. One of these, Hc1, is relatively well characterized and induces DNA condensation in vitro, whereas the other, Hc2, is functionally virtually uncharacterized. In this study we describe the purification of Hc2, and a detailed comparative functional analysis of Hc2 and Hc1 is presented. By gel shift assays and electron microscopy, marked differences in the nucleic acid-binding properties of Hc2 and Hc1 were observed. Furthermore, Hc2 was found to strongly inhibit translation and transcription in vitro. Our results imply that DNA condensation is not the only function of Hc2.

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