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

Melanie A. Adams-Cioaba, Joanne C. Krupa, Chao Xu, John S. Mort () and Jinrong Min ()
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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.
Jinrong Min: Structural Genomics Consortium, University of Toronto, 101 College Street, Toronto, Ontario M5G 1L7, Canada.

Nature Communications, 2011, vol. 2, issue 1, 1-8

Abstract: 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.

Date: 2011
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DOI: 10.1038/ncomms1204

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