Reassessment of protein stability, DNA binding, and protection of Mycobacterium smegmatis Dps.

@article{Ceci2005ReassessmentOP,
  title={Reassessment of protein stability, DNA binding, and protection of Mycobacterium smegmatis Dps.},
  author={Pierpaolo Ceci and Andrea Ilari and Elisabetta Falvo and Laura Giangiacomo and Emilia Chiancone},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 41},
  pages={34776-85}
}
The structure and function of Mycobacterium smegmatis Dps (DNA-binding proteins from starved cells) and of the protein studied by Gupta and Chatterji, in which the C terminus that is used for binding DNA contains a histidine tag, have been characterized in parallel. The native dodecamer dissociated reversibly into dimers above pH 7.5 and below pH 6.0, with apparent pK(a) values of approximately 7.65 and 4.75; at pH approximately 4.0, dimers formed monomers. Based on structural analysis, the two… CONTINUE READING

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