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A novel dnaK operon from Porphyromonas gingivalis
A Yoshida1, Y Nakano, Y Yamashita
1First Department of Oral and Maxillofacial Surgery, Faculty of Dentistry, Kyushu University, Fukuoka, Japan.
FEBS Letters
|April 1, 1999
Summary
Porphyromonas gingivalis DnaK functions within the DnaK chaperone system, despite lacking DnaJ and GrpE homologues in its operon. Its ATPase activity is enhanced by external DnaJ and GrpE, highlighting unique genetic adaptations.
Area of Science:
- Molecular Biology
- Microbiology
- Protein Biochemistry
Background:
- The dnaK operon is crucial for bacterial heat shock response.
- Porphyromonas gingivalis is a significant oral pathogen.
- Understanding bacterial chaperone systems is vital for pathogen control.
Purpose of the Study:
- To elucidate the genetic structure and functional characteristics of the dnaK operon in Porphyromonas gingivalis.
- To investigate the interaction of P. gingivalis DnaK with other chaperone components.
Main Methods:
- DNA sequencing of the P. gingivalis dnaK operon.
- Analysis of gene organization and transcription.
- In vitro assays to measure ATPase activity of P. gingivalis DnaK.
Main Results:
- The P. gingivalis dnaK operon lacks homologues for dnaJ and grpE but contains genes for small heat shock proteins.
- These genes are co-transcribed with dnaK.
- P. gingivalis DnaK ATPase activity showed a 40-fold synergistic stimulation with Escherichia coli DnaJ and GrpE.
Conclusions:
- P. gingivalis DnaK operates as part of the DnaK chaperone system, exhibiting unique genetic and evolutionary features.
- The findings suggest a functional DnaK chaperone system in P. gingivalis despite its distinct genetic organization.
- This study provides insights into the molecular mechanisms of heat shock response in this important pathogen.