Protein folding in Escherichia coli: the chaperonin GroE and its substrates.

@article{Masters2009ProteinFI,
  title={Protein folding in Escherichia coli: the chaperonin GroE and its substrates.},
  author={Millicent Masters and Garry Blakely and Andrew Coulson and N. R. Mclennan and Vollodymyr Yerko and J. R. Acord},
  journal={Research in microbiology},
  year={2009},
  volume={160 4},
  pages={
          267-77
        }
}
A brief summary of the role of DnaK and GroE chaperones in protein folding precedes a discussion of the role of GroE in Escherichia coli. We consider its obligate substrates, the 8 that are both obligate and essential, and the prospects for constructing a mutant that could survive without it. Structural features of GroE-dependent polypeptides are also considered. 
BETA

Figures, Tables, and Topics from this paper.

Similar Papers

Citations

Publications citing this paper.
SHOWING 1-10 OF 14 CITATIONS

Macromolecule-Assisted de novo Protein Folding

  • International journal of molecular sciences
  • 2012
VIEW 14 EXCERPTS
CITES BACKGROUND
HIGHLY INFLUENCED

Mechanism of methionine synthase overexpression in chaperonin-depleted Escherichia coli.

  • Microbiology
  • 2012
VIEW 6 EXCERPTS
CITES BACKGROUND & METHODS
HIGHLY INFLUENCED

References

Publications referenced by this paper.
SHOWING 1-10 OF 45 REFERENCES

GroE is vital for cell-wall synthesis

VIEW 11 EXCERPTS
HIGHLY INFLUENTIAL