Abstract
Human DJ-1 and Escherichia coli Hsp31 belong to ThiJ/PfpI family, whose members contain a conserved domain. DJ-1 is associated with autosomal recessive early onset parkinsonism and Hsp31 is a molecular chaperone. Structural comparisons between DJ-1, Hsp31, and an Archaea protease, a member of ThiJ/PfpI family, lead to the identification of the chaperone activity of DJ-1 and the proteolytic activity of Hsp31. Moreover, the comparisons provide insights into how the functional diversity is realized in proteins that share an evolutionarily conserved domain. On the basis of the chaperone activity the possible role of DJ-1 in the pathogenesis of Parkinson's disease is discussed.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Binding Sites
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Chemical Phenomena
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Chemistry, Physical
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Computer Simulation
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Conserved Sequence*
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Crystallization
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Dimerization
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Escherichia coli Proteins / chemistry*
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism
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Gene Deletion
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Humans
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Intracellular Signaling Peptides and Proteins
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Luciferases / metabolism
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Models, Molecular
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Molecular Chaperones / chemistry*
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Molecular Chaperones / genetics
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Molecular Chaperones / metabolism
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Molecular Sequence Data
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Molecular Structure
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Mutagenesis
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Nerve Tissue Proteins / genetics
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Oncogene Proteins / chemistry*
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Oncogene Proteins / genetics
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Oncogene Proteins / metabolism
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Oxidation-Reduction
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Parkinson Disease / genetics
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Peptide Fragments / genetics
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Peptide Hydrolases / metabolism
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Point Mutation
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Protein Deglycase DJ-1
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Protein Structure, Quaternary
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Synucleins
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Ubiquitin-Protein Ligases / genetics
Substances
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Escherichia coli Proteins
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Intracellular Signaling Peptides and Proteins
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Molecular Chaperones
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Nerve Tissue Proteins
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Oncogene Proteins
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Peptide Fragments
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Synucleins
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hchA protein, E coli
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Luciferases
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Ubiquitin-Protein Ligases
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parkin protein
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PARK7 protein, human
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Protein Deglycase DJ-1
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Peptide Hydrolases