Domain swapping oligomerization of thermostable c-type cytochrome in E. coli cells

@article{Hayashi2016DomainSO,
  title={Domain swapping oligomerization of thermostable c-type cytochrome in E. coli cells},
  author={Yugo Hayashi and Masaru Yamanaka and Satoshi Nagao and Hirofumi Komori and Yoshiki Higuchi and Shun Hirota},
  journal={Scientific Reports},
  year={2016},
  volume={6}
}
Knowledge on domain swapping in vitro is increasing, but domain swapping may not occur regularly in vivo, and its information in cells is limited. Herein, we show that domain-swapped oligomers of a thermostable c-type cytochrome, Hydrogenobacter thermophilus cyt c552, are formed in E. coli which expresses cyt c552. The region containing the N-terminal α-helix and heme was domain-swapped between protomers in the dimer formed in E. coli. The amount of cyt c552 oligomers increased in E. coli as… 
13 Citations
Protein surface charge effect on 3D domain swapping in cells for c-type cytochromes.
Formation and carbon monoxide‐dependent dissociation of Allochromatium vinosum cytochrome c′ oligomers using domain‐swapped dimers
TLDR
The results suggest that protein oligomer formation may be controlled by utilizing domain swapping for a dimer–monomer transition protein.
The Human Cytochrome c Domain-Swapped Dimer Facilitates Tight Regulation of Intrinsic Apoptosis.
TLDR
It is shown that the human DSD is kinetically more stable than horse and yeast DSDs and appears to have evolved into a pH-inducible switch that provides a means to control activation of apoptosis near pH 7.0.
Modulation of protein oligomerization: An overview.
Small Molecule-Induced Domain Swapping as a Mechanism for Controlling Protein Function and Assembly
Domain swapping is the process by which identical proteins exchange reciprocal segments to generate dimers. Here we introduce induced domain swapping (INDOS) as a mechanism for regulating protein
3D domain swapping of azurin from Alcaligenes xylosoxidans.
TLDR
It is found that azurin from Alcaligenes xylosoxidans oligomerizes by the procedure of 2,2,2-trifluoroethanol addition to Cu(i)-azurin at pH 5.0, lyophilization, and dissolution at pH 7.0; these results open the door for designing oligomers of blue copper proteins by domain swapping.
3D domain swapping of azurin from Alcaligenes xylosoxidans.
Protein oligomers have gained interest, owing to their increased knowledge in cells and promising utilization for future materials. Various proteins have been shown to 3D domain swap, but there has
Cytochrome c Can Form a Well-Defined Binding Pocket for Hydrocarbons.
TLDR
The dimer structure shows that only a modest deformation of monomeric cytochrome c would suffice to form the hydrocarbon binding site occupied by these detergents, and provides atomic resolution evidence for the extended lipid anchorage model for cy tochrome c/cardiolipin binding.
...
1
2
...

References

SHOWING 1-10 OF 56 REFERENCES
Domain-Swapped Dimer of Pseudomonas aeruginosa Cytochrome c 551: Structural Insights into Domain Swapping of Cytochrome c Family Proteins
TLDR
It is shown that the unstable loop region has a tendency to become a hinge loop in domain-swapped proteins, although the swapping region differed among proteins.
Domain swapping of the heme and N-terminal α-helix in Hydrogenobacter thermophilus cytochrome c(552) dimer.
TLDR
It is shown that the structural and thermodynamic properties of dimeric Hydrogenobacter thermophilus (HT) cytochrome c(552) (cyt c (552)) and dimeric horse cyt c are different, although both proteins belong to the cyt c superfamily.
Domain-swapped cytochrome cb562 dimer and its nanocage encapsulating a Zn-SO4 cluster in the internal cavity.
TLDR
The results show that domain swapping can be applied in the construction of unique protein nanostructures and heme attachment to the protein moiety stabilizes the domain-swapped structure.
Cytochrome c polymerization by successive domain swapping at the C-terminal helix
TLDR
It is found that cyt c forms polymers by successive domain swapping, where the C-terminal helix is displaced from its original position in the monomer and Met-heme coordination is perturbed significantly.
Change in structure and ligand binding properties of hyperstable cytochrome c555 from Aquifex aeolicus by domain swapping
TLDR
The results show that the ligand binding character of hyperstable AA cyt c555 changes upon dimerization by domain swapping, owing to the thermostability and pH tolerance of the dimer.
Formation of oligomeric cytochrome c during folding by intermolecular hydrophobic interaction between N- and C-terminal α-helices.
TLDR
The results show that cyt c oligomers are formed through intermolecular hydrophobic interaction between the N- and C-terminal α-helices during folding, and show that it is important to consider formation of domain-swapped oligomeric proteins when folding at high protein concentrations.
Foldon unfolding mediates the interconversion between Mpro-C monomer and 3D domain-swapped dimer
TLDR
It is proposed that there exists a special dimeric intermediate enabling the protein core to unpack and the α1-helices to swap in a hydrophobic environment, which minimizes the energy cost of the 3D domain-swapping process.
Formation of domain-swapped oligomer of cytochrome C from its molten globule state oligomer.
TLDR
Results indicate that a certain amount of molten globule state oligomers of cyt c convert to domain-swapped oligomers during refolding and that the intermolecular interactions necessary for domain swapping are present in the molten globules state.
Protein Folding Modulates the Swapped Dimerization Mechanism of Methyl-Accepting Chemotaxis Heme Sensors
TLDR
Analysis of the periplasmic sensor domains GSU0582 and GSU0935 provides evidence that the sensing threshold and intensity of the propagated allosteric effect is linked to the stability of the PAS-fold, as this property modulates domain swapping and dimerization.
...
1
2
3
4
5
...