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The Escherichia coli ribosomal protein S16 is an endonuclease

Authors

  • Jacques Oberto,

    1. lnstitut de Biologie Physico-chimique, Laboratoire de Physiologie Bactérienne, 13 rue Pierre et Marie Curie, 75005 Paris, France.
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    • These authors contributed equally to this work.

  • Eliette Bonnefoy,

    1. lnstitut de Biologie Physico-chimique, Laboratoire de Physiologie Bactérienne, 13 rue Pierre et Marie Curie, 75005 Paris, France.
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    • These authors contributed equally to this work.

  • Elisabeth Mouray,

    1. lnstitut de Biologie Physico-chimique, Laboratoire de Physiologie Bactérienne, 13 rue Pierre et Marie Curie, 75005 Paris, France.
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  • Olivier Pellegrini,

    1. lnstitut de Biologie Physico-chimique, Laboratoire de Physiologie Bactérienne, 13 rue Pierre et Marie Curie, 75005 Paris, France.
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  • P. Mikael Wikström,

    1. Department of Microbiology, University of Umeâ, S901 87 Umeâ, Sweden.
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  • Josette Rouvière-Yaniv

    Corresponding author
    1. lnstitut de Biologie Physico-chimique, Laboratoire de Physiologie Bactérienne, 13 rue Pierre et Marie Curie, 75005 Paris, France.
    • For correspondence. Tel. (1) 43 25 26 09; Fax (1) 40 46 83 31.

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Summary

The histone-like protein HU isolated from Escherichia coli exhibited, after several purification steps, a Mg2+-dependent nuclease activity. We show here that this activity can be dissociated from HU by a denaturation-renaturation step, and is due to a small fraction of ribosomal protein S16 co-purifying with HU. S16 is an essential component of the 30S ribosomal particles. We have cloned, overproduced, and purified a histidine-tagged S16 and shown that this protein is a DNA-binding protein carrying a Mg2+-Mn2+-dependent endonuclease activity. This is an unexpected property for a ribosomal protein.

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