The Hsc66-Hsc20 chaperone system in Escherichia coli: chaperone activity and interactions with the DnaK-DnaJ-grpE system.

@article{Silberg1998TheHC,
  title={The Hsc66-Hsc20 chaperone system in Escherichia coli: chaperone activity and interactions with the DnaK-DnaJ-grpE system.},
  author={J. Silberg and K. Hoff and L. Vickery},
  journal={Journal of bacteriology},
  year={1998},
  volume={180 24},
  pages={
          6617-24
        }
}
  • J. Silberg, K. Hoff, L. Vickery
  • Published 1998
  • Biology, Medicine
  • Journal of bacteriology
    • Hsc66, a stress-70 protein, and Hsc20, a J-type accessory protein, comprise a newly described Hsp70-type chaperone system in addition to DnaK-DnaJ-GrpE in Escherichia coli. Because endogenous substrates for the Hsc66-Hsc20 system have not yet been identified, we investigated chaperone-like activities of Hsc66 and Hsc20 by their ability to suppress aggregation of denatured model substrate proteins, such as rhodanese, citrate synthase, and luciferase. Hsc66 suppressed aggregation of rhodanese and… CONTINUE READING
    View PDF
    76 Citations
    Highly Influencial Citations
    5
    Background Citations
    22
    Methods Citations
    3
    Results Citations
    2
    76 Citations
    Citation Type

    Citation Type

    Hsc62, Hsc56, and GrpE, the third Hsp70 chaperone system of Escherichia coli.
    • 23
    Structure-Function Analysis of HscC, theEscherichia coli Member of a Novel Subfamily of Specialized Hsp70 Chaperones*
    • 38
    • PDF
    Regulation of the HscA ATPase Reaction Cycle by the Co-chaperone HscB and the Iron-Sulfur Cluster Assembly Protein IscU*
    • 76
    • PDF
    Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli.
    • 206
    • PDF
    Molecular Chaperones HscA/Ssq1 and HscB/Jac1 and Their Roles in Iron-Sulfur Protein Maturation
    • 143
    DjlA Is a Third DnaK Co-chaperone of Escherichia coli, and DjlA-mediated Induction of Colanic Acid Capsule Requires DjlA-DnaK Interaction*
    • 57
    • PDF
    Correction to The Specialized Hsp70 (HscA) Interdomain Linker Binds to Its Nucleotide-Binding Domain and Stimulates ATP Hydrolysis in Both cis and trans Configurations
    • 8
    The Fe/S Assembly Protein IscU Behaves as a Substrate for the Molecular Chaperone Hsc66 from Escherichia coli *
    • 103
    • PDF
    The Pseudomonas aeruginosa hscA gene encodes Hsc66, a DnaK homologue.
    • 12
    The ATPase domain of HscC (DnaK homolog) is essential for interfering sigma70 activity in E. coli.
    • 4
    • Highly Influenced
    • PDF

    References

    SHOWING 1-10 OF 69 REFERENCES
    Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli
    • 92
    Regulation of the Heat-shock Protein 70 Reaction Cycle by the Mammalian DnaJ Homolog, Hsp40*
    • 324
    • PDF
    The DnaK Chaperone System of Escherichia coli: Quaternary Structures and Interactions of the DnaK and GrpE Components (*)
    • 158
    • PDF
    DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat‐induced protein damage.
    • 547
    The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE.
    • 475
    • PDF
    Purification and Biochemical Properties of Saccharomyces cerevisiae Mdj1p, the Mitochondrial DnaJ Homologue*
    • 24
    • Highly Influential
    • PDF
    A gene encoding a DnaK/hsp70 homolog in Escherichia coli.
    • B. Seaton, L. Vickery
    • Biology, Medicine
    • Proceedings of the National Academy of Sciences of the United States of America
    • 1994
    • 89
    • PDF
    A Bipartite Signaling Mechanism Involved in DnaJ-mediated Activation of the Escherichia coli DnaK Protein (*)
    • 200
    • PDF
    The Conserved G/F Motif of the DnaJ Chaperone Is Necessary for the Activation of the Substrate Binding Properties of the DnaK Chaperone (*)
    • 124
    • PDF
    The role of ATP in the functional cycle of the DnaK chaperone system.
    • 380