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Review
. 2006 Dec;174(4):1699-707.
doi: 10.1534/genetics.104.68262.

Toothpicks, serendipity and the emergence of the Escherichia coli DnaK (Hsp70) and GroEL (Hsp60) chaperone machines

Costa Georgopoulos  1
Affiliations
Review

Toothpicks, serendipity and the emergence of the Escherichia coli DnaK (Hsp70) and GroEL (Hsp60) chaperone machines

Costa Georgopoulos. Genetics. 2006 Dec.
No abstract available

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Figures

F<sc>igure</sc> 1.—
Figure 1.—
The genetic strategy used to isolate the E. coli Gro mutants. The diagram shows the effect of increasing phage concentrations on bacterial growth and colony morphology. See text and Georgopoulos (1971) for details.
F<sc>igure</sc> 2.—
Figure 2.—
The original diagram used by Ira and me during the 1970 Cold Spring Harbor meeting on phage λ to rationalize the apparent allele specificity observed between some of the E. coli groP mutants and the corresponding phage λP compensatory mutations.
F<sc>igure</sc> 3.—
Figure 3.—
Role of DnaK and GroE chaperone machines in nascent protein folding. The diagram depicts the ribosome, the ribosome-bound TF chaperone, and the DnaK/DnaJ/GrpE and GroES/GroEL chaperone machines. The diagram depicts the various pathways that nascent polypeptides may follow during the intracellular folding process to arrive at their native state (N). It is essentially adapted from Hartl and Hayer-Hartl (2002), except all structures are drawn to scale. See text for details.
See this image and copyright information in PMC

References

    1. Ang, D., and C. Georgopoulos, 1989. The heat-shock-regulated grpE gene of Escherichia coli is required for bacterial growth at all temperatures but is dispensable in certain mutant backgrounds. J. Bacteriol. 171: 2748–2755. - PMC - PubMed
    1. Ang, D., G. N. Chandrasekhar, M. Zylicz and C. Georgopoulos, 1986. Escherichia coli grpE gene codes for heat shock protein B25.3, essential for both lambda DNA replication at all temperatures and host growth at high temperature. J. Bacteriol. 167: 25–29. - PMC - PubMed
    1. Ang, D., K. Liberek, D. Skowyra, M. Zylicz and C. Georgopoulos, 1991. Biological role and regulation of the universally conserved heat shock proteins. J. Biol. Chem. 266: 24233–24236. - PubMed
    1. Ang, D., F. Keppel, G. Klein, A. Richardson and C. Georgopoulos, 2000. Genetic analysis of bacteriophage-encoded cochaperonins. Annu. Rev. Genet. 34: 439–456. - PubMed
    1. Ang, D., A. Richardson, M. P. Mayer, F. Keppel, H. Krisch et al., 2001. Pseudo-T-even bacteriophage RB49 encodes CocO, a cochaperonin for GroEL, which can substitute for Escherichia coli's GroES and bacteriophage T4's Gp31. J. Biol. Chem. 276: 8720–8726. - PubMed

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