Understanding Cold Adaptation in Shewanella sp. SIB1 through FK506-Binding Protein 22
Author Information
Author(s): Budiman Cahyo, Koga Yuichi, Takano Kazufumi, Kanaya Shigenori
Primary Institution: Osaka University
Hypothesis
The study investigates the role of FK506-binding protein 22 in the cold adaptation of Shewanella sp. SIB1.
Conclusion
SIB1 FKBP22 assists in protein folding at low temperatures, acting as both a foldase and a chaperone.
Supporting Evidence
- SIB1 FKBP22 is significantly expressed at low temperatures, indicating its role in cold adaptation.
- The protein exhibits increased catalytic efficiency at low temperatures.
- SIB1 FKBP22 can bind to folding intermediate proteins, demonstrating its chaperone activity.
- Structural analysis suggests that SIB1 FKBP22 has a V-shaped homodimeric structure.
- Cold-adapted enzymes like SIB1 FKBP22 show reduced stability at higher temperatures.
Takeaway
This study shows that a special protein helps bacteria survive in cold environments by making sure their other proteins fold correctly.
Methodology
The study involved structural and functional analyses of SIB1 FKBP22, including PPIase activity assays and binding studies.
Limitations
The study primarily focuses on one protein and does not explore other potential mechanisms of cold adaptation in Shewanella sp. SIB1.
Digital Object Identifier (DOI)
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