Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli.

@article{Yoo1996PurificationAC,
  title={Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli.},
  author={S J Yoo and Jae Hong Seol and Dong Hae Shin and Markus Rohrwild and Min Suk Kang and Keiji Tanaka and Alfred L Goldberg and Chin Ha Chung},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 24},
  pages={14035-40}
}
The hslVU operon in Escherichia coli encodes two heat shock proteins, HslV, a 19-kDa protein homologous to beta-type subunits of the 20 S proteasomes, and HslU, a 50-kDa protein related to the ATPase ClpX. We have recently shown that HslV and HslU can function together as a novel ATP-dependent protease, the HslVU protease. We have now purified both proteins to apparent homogeneity from extracts of E. coli carrying the hslVU operon on a multicopy plasmid. HslU by itself cleaved ATP, and pure… CONTINUE READING