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Dissociation kinetics of the GroEL-gp31 chaperonin complex studied with Förster resonance energy transfer.

Publication ,  Journal Article
Calmat, S; Hendriks, J; van Heerikhuizen, H; Schmidt, CF; van der Vies, SM; Peterman, EJG
Published in: Biochemistry
December 2009

Propagation of bacteriophage T4 in its host Escherichia coli involves the folding of the major capsid protein gp23, which is facilitated by a hybrid chaperone complex consisting of the bacterial chaperonin GroEL and the phage-encoded co-chaperonin, gp31. It has been well established that the GroEL-gp31 complex is capable of folding gp23 whereas the homologous GroEL-GroES complex cannot perform this function. To assess whether this is a consequence of differences in the interactions of the proteins within the chaperonin complex, we have investigated the dissociation kinetics of GroEL-gp31 and GroEL-GroES complexes using Forster resonance energy transfer. Here we report that the dissociation of gp31 from GroEL is slightly faster than that of GroES from GroEL and is further accelerated by the binding of gp23. In contrast to what had been observed previously, we found that gp23 is able to interact with the GroEL-GroES complex, which might explain how bacteriophage T4 redirects the folding machinery of Escherichia coli during morphogenesis.

Duke Scholars

Published In

Biochemistry

DOI

EISSN

1520-4995

ISSN

0006-2960

Publication Date

December 2009

Volume

48

Issue

49

Start / End Page

11692 / 11698

Related Subject Headings

  • Viral Proteins
  • Protein Interaction Mapping
  • Protein Folding
  • Kinetics
  • Fluorescence Resonance Energy Transfer
  • Escherichia coli
  • Chaperonin 60
  • Chaperonin 10
  • Capsid Proteins
  • Biochemistry & Molecular Biology
 

Citation

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Calmat, S., Hendriks, J., van Heerikhuizen, H., Schmidt, C. F., van der Vies, S. M., & Peterman, E. J. G. (2009). Dissociation kinetics of the GroEL-gp31 chaperonin complex studied with Förster resonance energy transfer. Biochemistry, 48(49), 11692–11698. https://doi.org/10.1021/bi9013962
Calmat, Stéphane, Johnny Hendriks, Harm van Heerikhuizen, Christoph F. Schmidt, Saskia M. van der Vies, and Erwin J. G. Peterman. “Dissociation kinetics of the GroEL-gp31 chaperonin complex studied with Förster resonance energy transfer.Biochemistry 48, no. 49 (December 2009): 11692–98. https://doi.org/10.1021/bi9013962.
Calmat S, Hendriks J, van Heerikhuizen H, Schmidt CF, van der Vies SM, Peterman EJG. Dissociation kinetics of the GroEL-gp31 chaperonin complex studied with Förster resonance energy transfer. Biochemistry. 2009 Dec;48(49):11692–8.
Calmat, Stéphane, et al. “Dissociation kinetics of the GroEL-gp31 chaperonin complex studied with Förster resonance energy transfer.Biochemistry, vol. 48, no. 49, Dec. 2009, pp. 11692–98. Epmc, doi:10.1021/bi9013962.
Calmat S, Hendriks J, van Heerikhuizen H, Schmidt CF, van der Vies SM, Peterman EJG. Dissociation kinetics of the GroEL-gp31 chaperonin complex studied with Förster resonance energy transfer. Biochemistry. 2009 Dec;48(49):11692–11698.
Journal cover image

Published In

Biochemistry

DOI

EISSN

1520-4995

ISSN

0006-2960

Publication Date

December 2009

Volume

48

Issue

49

Start / End Page

11692 / 11698

Related Subject Headings

  • Viral Proteins
  • Protein Interaction Mapping
  • Protein Folding
  • Kinetics
  • Fluorescence Resonance Energy Transfer
  • Escherichia coli
  • Chaperonin 60
  • Chaperonin 10
  • Capsid Proteins
  • Biochemistry & Molecular Biology