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Structural basis for the recognition and cleavage of histone H3 by cathepsin L

Author

Listed:
  • Melanie A. Adams-Cioaba

    (Structural Genomics Consortium, University of Toronto, 101 College Street, Toronto, Ontario M5G 1L7, Canada.)

  • Joanne C. Krupa

    (Genetics Unit, Shriners Hospital for Children, 1529 Cedar Avenue, Montreal, Quebec H3G 1A6, Canada.)

  • Chao Xu

    (Structural Genomics Consortium, University of Toronto, 101 College Street, Toronto, Ontario M5G 1L7, Canada.)

  • John S. Mort

    (Genetics Unit, Shriners Hospital for Children, 1529 Cedar Avenue, Montreal, Quebec H3G 1A6, Canada.
    McGill University)

  • Jinrong Min

    (Structural Genomics Consortium, University of Toronto, 101 College Street, Toronto, Ontario M5G 1L7, Canada.
    University of Toronto)

Abstract

Proteolysis of eukaryotic histone tails has emerged as an important factor in the modulation of cell-cycle progression and cellular differentiation. The recruitment of lysosomal cathepsin L to the nucleus where it mediates proteolysis of the mouse histone H3 tail has been described recently. Here, we report the three-dimensional crystal structures of a mature, inactive mutant of human cathepsin L alone and in complex with a peptide derived from histone H3. Canonical substrate–cathepsin L interactions are observed in the complex between the protease and the histone H3 peptide. Systematic analysis of the impact of posttranslational modifications at histone H3 on substrate selectivity suggests cathepsin L to be highly accommodating of all modified peptides. This is the first report of cathepsin L–histone H3 interaction and the first structural description of cathepsin L in complex with a substrate.

Suggested Citation

  • Melanie A. Adams-Cioaba & Joanne C. Krupa & Chao Xu & John S. Mort & Jinrong Min, 2011. "Structural basis for the recognition and cleavage of histone H3 by cathepsin L," Nature Communications, Nature, vol. 2(1), pages 1-8, September.
    • Handle: RePEc:nat:natcom:v:2:y:2011:i:1:d:10.1038_ncomms1204
    DOI: 10.1038/ncomms1204
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