Investigation of ClpXP Protease Mechanism of Function and its Interaction with the Folding Chaperone Trigger Factor

@inproceedings{Yu2013InvestigationOC,
  title={Investigation of ClpXP Protease Mechanism of Function and its Interaction with the Folding Chaperone Trigger Factor},
  author={Angela Yeou Hsiung Yu},
  year={2013}
}
The major chaperones identified in Escherichia coli that assist in protein folding include trigger factor (TF), DnaK/DnaJ/GrpE and GroEL/GroES systems. The main ATP-dependent proteases are ClpXP, ClpAP, HslUV, Lon, and FtsH. From detailed sequence analysis, we found that tig (gene for TF), clpX, and clpP genes co-localize next to each other in most examined bacteria. We hypothesized that TF and ClpXP are functionally associated. TF is a ribosome-associated folding chaperone whereas ClpXP is a… CONTINUE READING

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