Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis.

Tilly, Kit; Murialdo, Helios; Georgopoulos, Costa

doi:10.1073/pnas.78.3.1629

Cited by 151 publications

(95 citation statements)

References 21 publications

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“…The results identified the formation of all the stable complexes of GroEL with the bound components, and the bands in each lane appear at MM positions of the expected components. The band of GroES subunit appeared above the lysozyme band at the position corresponding to an apparent MM of 15 kDa but not 10 kDa as also noted by Tilly et al (25). The order of addition of the ligands had no effect on the formation of all the ternary complexes.…”

Section: Identification Of Complexes Of Groel With Different Ligands-bysupporting

confidence: 76%

“Half of the Sites” Binding ofd-Glyceraldehyde-3-phosphate Dehydrogenase Folding Intermediate with GroEL

Wang

1999

Journal of Biological Chemistry

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Section: Identification Of Complexes Of Groel With Different Ligands-bysupporting

confidence: 76%

“Half of the Sites” Binding ofd-Glyceraldehyde-3-phosphate Dehydrogenase Folding Intermediate with GroEL

Wang

1999

Journal of Biological Chemistry

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“…It was shown that the glycine residues are needed to ensure flexibility required for the mobile loop ␤ hairpin conformation (15,16). However, bacteria containing GroES with mutations in Gly-24 were viable, suggesting that perhaps one glycine at this position is sufficient for function of GroES (16,27,28). Consistent with these reports, the GroES mutant G24A was equally as active as wild type GroES at room temperature with a similar EC 50 , and was able to inhibit GroEL ATPase (Table 1; Fig.…”

Section: Purification and Structural Properties Of Wild Type Andmentioning

confidence: 99%

Significance of the N-terminal Domain for the Function of Chloroplast cpn20 Chaperonin

Bonshtien

Weiss

Vitlin

et al. 2007

Journal of Biological Chemistry

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Chaperonins cpn60 and cpn10 are essential proteins involved in cellular protein folding. Plant chloroplasts contain a unique version of the cpn10 co-chaperonin, cpn20, which consists of two homologous cpn10-like domains (N-cpn20 and C-cpn20) that are connected by a short linker region. Although cpn20 seems to function like other single domain cpn10 oligomers, the structure and specific functions of the domains are not understood. We mutated amino acids in the "mobile loop" regions of N-cpn20, C-cpn20 or both: a highly conserved glycine, which was shown to be important for flexibility of the mobile loop, and a leucine residue shown to be involved in binding of co-chaperonin to chaperonin. The mutant proteins were purified and their oligomeric structure validated by gel filtration, native gel electrophoresis, and circular dichroism. Functional assays of protein refolding and inhibition of GroEL ATPase both showed (i) mutation of the conserved glycine reduced the activity of cpn20, whether in N-cpn20 (G32A) or C-cpn20 (G130A). The same mutation in the bacterial cpn10 (GroES G24A) had no effect on activity. (ii) Mutations in the highly conserved leucine of N-cpn20 (L35A) and in the corresponding L27A of GroES resulted in inactive protein. (iii) In contrast, mutant L133A, in which the conserved leucine of C-cpn20 was altered, retained 55% activity. We conclude that the structure of cpn20 is much more sensitive to alterations in the mobile loop than is the structure of GroES. Moreover, only N-cpn20 is necessary for activity of cpn20. However, full and efficient functioning requires both domains.

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“…Certain unfolded or partially folded polypeptides bind to GroEL, a double-toroid, tetradecameric protein composed of 58-kDa subunits arranged with 7-fold symmetry (3)(4)(5). GroES, made up of 10.5-kDa subunits arranged in 7-fold symmetry (6,7), binds to GroEL, thus stabilizing a conformational change that doubles the substrate-containing cavity of GroEL and promoting the release of the substrate into the cavity (8,9). The amount of time the substrate spends in the cavity depends on the rate of ATP hydrolysis in the GroEL cis ring and the release of GroES (10,11).…”

mentioning

confidence: 99%

Compensatory Changes in GroEL/Gp31 Affinity as a Mechanism for Allele-specific Genetic Interaction

Richardson

Vies

Taher

et al. 1999

Journal of Biological Chemistry

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Previous work has shown that the GroEL-GroES interaction is primarily mediated by the GroES mobile loop. In bacteriophage T4 infection, GroES is substituted by the gene 31-encoded cochaperonin, Gp31. Using a genetic selection scheme, we have identified a new set of mutations in gene 31 that affect interaction with GroEL; all mutations result in changes in the mobile loop of Gp31. Biochemical analyses reveal that the mobile loop mutations alter the affinity between Gp31 and GroEL, most likely by modulating the stability of the GroEL-bound hairpin conformation of the mobile loop. Surprisingly, mutations in groEL that display allele-specific interactions with mutations in gene 31 alter residues in the GroEL intermediate domain, distantly located from the mobile loop binding site. The observed patterns of genetic and biochemical interaction between GroES or Gp31 and GroEL point to a mechanism of genetic allele specificity based on compensatory changes in affinity of the protein-protein interaction. Mutations studied in this work indirectly alter affinity by modulating a folding transition in the Gp31 mobile loop or by modulating a hinged conformational change in GroEL.

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Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis.

Abstract: Previous-work has uncovered the existence of an Escherichia coli locus, groE, that is essential for bacterial growth,

Cited by 151 publications

References 21 publications

“Half of the Sites” Binding ofd-Glyceraldehyde-3-phosphate Dehydrogenase Folding Intermediate with GroEL

“Half of the Sites” Binding ofd-Glyceraldehyde-3-phosphate Dehydrogenase Folding Intermediate with GroEL

Significance of the N-terminal Domain for the Function of Chloroplast cpn20 Chaperonin

Compensatory Changes in GroEL/Gp31 Affinity as a Mechanism for Allele-specific Genetic Interaction

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