
ClpX is a member of Hsp100 (heat-shock protein) family which is conserved among organisms. Hsp100/ Clp implicates in stress resistance, intracellular protein turn-over, DNA replication and regulation of gene expression. Tuberculosis remains one of the major threats to human health. In pathogens, ClpX protease plays an important role in the gene expression regulation, pathogenesis, and resistance of immune stress. The structure, substrates and target genes of ClpX are summarized in this study. The biological function of M. tuberculosis ClpX, such as gene expression regulation, pathogenesis, intracellular survival and persistence, evolution and structural feature, substrates is the focus of this summary.
Adenosine Triphosphatases, Hydrolases, Protein Conformation, Escherichia coli Proteins, Molecular Sequence Data, Serine Endopeptidases, Endopeptidase Clp, Gene Expression Regulation, Bacterial, Blotting, Northern, Escherichia coli, ATPases Associated with Diverse Cellular Activities, Humans, Amino Acid Sequence, Heat-Shock Proteins, Molecular Chaperones
Adenosine Triphosphatases, Hydrolases, Protein Conformation, Escherichia coli Proteins, Molecular Sequence Data, Serine Endopeptidases, Endopeptidase Clp, Gene Expression Regulation, Bacterial, Blotting, Northern, Escherichia coli, ATPases Associated with Diverse Cellular Activities, Humans, Amino Acid Sequence, Heat-Shock Proteins, Molecular Chaperones
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