Inter-ring Communication Allows the GroEL Chaperonin Complex to Distinguish Between Different Substrates

Overview

Journal Protein Sci

Specialty Biochemistry

Date 2007 Apr 26

PMID 17456746

Citations 11

Authors

Esther van Duijn

Albert J R Heck

Saskia M van der Vies

Affiliations

Soon will be listed here.

Abstract

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 inter-ring 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.

Citing Articles

Structural basis of substrate progression through the bacterial chaperonin cycle.

Gardner S, Darrow M, Lukoyanova N, Thalassinos K, Saibil H Proc Natl Acad Sci U S A. 2023; 120(50):e2308933120.

PMID: 38064510 PMC: 10723157. DOI: 10.1073/pnas.2308933120.

Cryo-EM structures of GroEL:ES with RuBisCO visualize molecular contacts of encapsulated substrates in a double-cage chaperonin.

Kim H, Park J, Lim S, Jun S, Jung M, Roh S iScience. 2022; 25(1):103704.

PMID: 35036883 PMC: 8749442. DOI: 10.1016/j.isci.2021.103704.

GroEL Mediates Folding of Serine/Threonine Protein Kinase, PrkC.

Virmani R, Singh Y, Hasija Y Indian J Microbiol. 2018; 58(4):520-524.

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A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperonin.

Natesh R, Clare D, Farr G, Horwich A, Saibil H Int J Biol Macromol. 2018; 118(Pt A):671-675.

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Distinct Stabilities of the Structurally Homologous Heptameric Co-Chaperonins GroES and gp31.

Dyachenko A, Tamara S, Heck A J Am Soc Mass Spectrom. 2018; 30(1):7-15.

PMID: 29736602 PMC: 6318259. DOI: 10.1007/s13361-018-1910-5.

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