title: [Bacterial ClpX protease structure and function--a review].
abstract: 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.
authors.affiliation: Institute of Modern Biopharmaceuticals, School of Life Sciences, Southwest University, Chongqing 400715, China. sonya85@swu.edu.cn
authors.forename: Lin
authors.initials: L
authors.lastname: Wang
authors.forename: Jianping
authors.initials: J
authors.lastname: Xie
mesh_terms: D000074183:ATPases Associated with Diverse Cellular Activities; D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D000595:Amino Acid Sequence; D015152:Blotting, Northern; D049071:Endopeptidase Clp / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D015964:Gene Expression Regulation, Bacterial; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000502:physiology; D006801:Humans; D006867:Hydrolases / Q000737:chemistry / Q000502:physiology; D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012697:Serine Endopeptidases / Q000737:chemistry / Q000502:physiology
chemical_list: D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D006867:Hydrolases; D012697:Serine Endopeptidases; D049071:Endopeptidase Clp; D000251:Adenosine Triphosphatases; C088072:ClpX protein, E coli; D000074183:ATPases Associated with Diverse Cellular Activities