Regulation of SulA cleavage by Lon protease by the C-terminal amino acid of SulA, histidine.

@article{Ishii2001RegulationOS,
  title={Regulation of SulA cleavage by Lon protease by the C-terminal amino acid of SulA, histidine.},
  author={Yoshiyuki Ishii and Fumio Amano},
  journal={The Biochemical journal},
  year={2001},
  volume={358 Pt 2},
  pages={473-80}
}
SulA protein, a cell division inhibitor in Escherichia coli, is degraded by Lon protease. The C-terminal eight residues of SulA have been shown to be recognized by Lon; however, it remains to be elucidated which amino acid in the C-terminus of SulA is critical for the recognition of SulA by Lon. To clarify this point, we constructed mutants of SulA with changes in the C-terminal residues, and examined the accumulation and stability of the resulting mutant SulA proteins in vivo. Substitution of… CONTINUE READING
20 Citations
36 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 20 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 36 references

The ClpXP and ClpAP

  • S. Gottesman, E. Roche, Y. Zhou, R. T. Sauer
  • 1998

Similar Papers

Loading similar papers…