The versatile mutational "repertoire" of Escherichia coli GroEL, a multidomain chaperonin nanomachine.

ABSTRACT: The bacterial chaperonins are highly sophisticated molecular nanomachines, controlled by the hydrolysis of ATP to dynamically trap and remove from the environment unstable protein molecules that are susceptible to denaturation and aggregation. Chaperonins also act to assist in the refolding of these unstable proteins, providing a means by which these proteins may return in active form to the complex environment of the cell. The Escherichia coli GroE chaperonin system is one of the largest protein supramolecular complexes known, whose quaternary structure is required for segregating aggregation-prone proteins. Over the course of more than two decades of research on GroE, it has become accepted that GroE, more specifically the GroEL subunit, is a "high-tolerance" molecular system, capable of

SUBMITTER: Mizobata T 

PROVIDER: S-EPMC5899694 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature