Limited proteolysis of E. coli ATP-dependent protease Lon - a unified view of the subunit architecture and characterization of isolated enzyme fragments.

@article{Melnikov2008LimitedPO,
  title={Limited proteolysis of E. coli ATP-dependent protease Lon - a unified view of the subunit architecture and characterization of isolated enzyme fragments.},
  author={Edward E. Melnikov and Anna G Andrianova and Andrey D Morozkin and Anton A Stepnov and Oksana V Makhovskaya and Istvan Botos and Alla Gustchina and Alexander Wlodawer and Tatyana V. Rotanova},
  journal={Acta biochimica Polonica},
  year={2008},
  volume={55 2},
  pages={281-96}
}
We carried out chymotryptic digestion of multimeric ATP-dependent Lon protease from Escherichia coli. Four regions sensitive to proteolytic digestion were located in the enzyme and several fragments corresponding to the individual structural domains of the enzyme or their combinations were isolated. It was shown that (i) unlike the known AAA(+) proteins, the ATPase fragment (A) of Lon has no ATPase activity in spite of its ability to bind nucleotides, and it is monomeric in solution regardless… CONTINUE READING