Isolation and Characterisation of Mutants of GroEL that are Fully Functional as Single Rings

Sun, Zhe; Scott, David J.; Lund, Peter A.

doi:10.1016/s0022-2836(03)00830-1

Cited by 52 publications

(55 citation statements)

References 48 publications

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“…If the same would hold true for the GroELgp31 system, a trans-folding mechanism would most likely not be able to supply the ''folding power'' required during T4 infection. Finally, Sun et al (35) have produced a set of single-ring GroEL mutants that support the growth of bacteriophage T4. These mutants form a chaperonin containing only a single cavity, hence, trans-folding is not possible, and gp23 must be folded in cis.…”

Section: Discussionmentioning

confidence: 99%

The T4-encoded cochaperonin, gp31, has unique properties that explain its requirement for the folding of the T4 major capsid protein

Bakkes

Faber

Heerikhuizen

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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The morphogenesis of bacteriophage T4 requires a specialized bacteriophage-encoded molecular chaperone (gp31) that is essential for the folding of the T4 major capsid protein (gp23). gp31 is related to GroES, the chaperonin of the Escherichia coli host because it displays a similar overall structure and properties. Why GroES is unable to fold the T4 capsid protein in conjunction with GroEL is unknown. Here we show that gp23 binds to the GroEL heptameric ring opposite to the ring that is bound by gp31 (the so-called trans-ring), while no binding to the trans-ring of the GroEL-GroES complex is observed. Although gp23 can be enclosed within the folding cage of the GroEL-gp31 complex, encapsulation within the GroEL-GroES complex is not possible. So it appears that folding of the T4 major capsid protein requires a gp31-dependent cis-folding mechanism likely inside an enlarged ''Anfinsen cage'' provided by GroEL and gp31.chaperones ͉ protein folding ͉ viral capsid assembly

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Section: Discussionmentioning

confidence: 99%

The T4-encoded cochaperonin, gp31, has unique properties that explain its requirement for the folding of the T4 major capsid protein

Bakkes

Faber

Heerikhuizen

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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“…In this model, the chromosomal groE promoter has been replaced by the pBAD promoter from the arabinose operon, which means that synthesis of native GroEL and GroES is completely repressed by the presence of glucose but can be induced in the presence of arabinose. This allows the ability of heterologous or mutant chaperonins to chaperone the folding of GroELdependent proteins in vivo to be determined (36). Constructs expressing the M. tuberculosis chaperonin proteins from the strong trc promoter were transformed into E. coli MGM100 to examine if they supported cell growth and therefore functioned as molecular chaperones.…”

Section: Vol 76 2008mentioning

confidence: 99%

AMycobacterium tuberculosisMutant Lacking thegroELHomologuecpn60.1Is Viable but Fails To Induce an Inflammatory Response in Animal Models of Infection

et al. 2008

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The causative agent of tuberculosis, Mycobacterium tuberculosis, has two chaperonin (Cpn60) proteins and one cochaperonin (Cpn10) protein. We show here that cpn60.2 and cpn10, but not cpn60.1, are essential for cell survival. A mutant lacking Cpn60.1 was indistinguishable from the wild-type organism in plate and broth culture and within murine macrophages, although it showed increased sensitivity to high temperature (55°C). However, infection of mice with the ⌬cpn60.1 mutant revealed a major difference from the wild-type organism. In spite of having equal numbers of bacteria in infected sites, the ⌬cpn60.1 mutant failed to produce granulomatous inflammation in either mice or guinea pigs. This was associated with reduced cytokine expression in infected animals and macrophages. Cell wall lipid acid composition was not altered in the mutant strain. Thus, it appears that Cpn60

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“…However, SR1 is unable to release GroES because the binding of ATP to the opposite trans-ring that triggers the co-chaperonin to dissociate from the complex is obviously not possible. Consequently, SR1 does not allow the release of properly folded proteins (Weissman et al 1995;Rye et al 1997;Sun et al 2003).…”

mentioning

confidence: 99%

Inter‐ring communication allows the GroEL chaperonin complex to distinguish between different substrates

2007

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The productive folding of substrate proteins by the GroEL complex of Escherichia coli requires the activity of both the chaperonin rings. These heptameric rings were shown to regulate the chaperonins' affinity for substrates and co-chaperonin via inter-ring communications; however, the molecular details of the interactions are not well understood. We have investigated the effect of substrate binding on interring communications of the chaperonin complex, both the double-ring GroEL as well as the single-ring SR1 chaperonin in complex with four different substrates by using mass spectrometry. This approach shows that whereas SR1 is unable to distinguish between Rubisco, gp23, gp5, and MDH, GroEL shows clear differences upon binding these substrates. The most distinctive binding behavior is observed for Rubisco, which only occupies one GroEL ring. Both bacteriophage capsid proteins (gp23 and gp5) as well as MDH are able to bind to the two GroEL rings simultaneously. Our data suggest that inter-ring communication allows the chaperonin complex to differentiate between substrates. Using collision induced dissociation in the gas phase, differences between the chaperonin(substrate) complexes are observed only when both rings are present. The data indicate that the size of the substrate is an important factor that determines the degree of stabilization of the chaperonin complex.

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Isolation and Characterisation of Mutants of GroEL that are Fully Functional as Single Rings

Cited by 52 publications

References 48 publications

The T4-encoded cochaperonin, gp31, has unique properties that explain its requirement for the folding of the T4 major capsid protein

The T4-encoded cochaperonin, gp31, has unique properties that explain its requirement for the folding of the T4 major capsid protein

AMycobacterium tuberculosisMutant Lacking thegroELHomologuecpn60.1Is Viable but Fails To Induce an Inflammatory Response in Animal Models of Infection

Inter‐ring communication allows the GroEL chaperonin complex to distinguish between different substrates

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