Single-Ring Intermediates Are Essential for Some Chaperonins

Overview

Journal Front Mol Biosci

Specialty Biology

Date 2018 May 15

PMID 29755985

Citations 8

Authors

Jay M Bhatt

Adrian S Enriquez

Jinliang Wang

Humberto M Rojo

Sudheer K Molugu

Zacariah L Hildenbrand

Ricardo A Bernal

Affiliations

Soon will be listed here.

Abstract

Chaperonins are macromolecular complexes found throughout all kingdoms of life that assist unfolded proteins reach a biologically active state. Historically, chaperonins have been classified into two groups based on sequence, subunit structure, and the requirement for a co-chaperonin. Here, we present a brief review of chaperonins that can form double- and single-ring conformational intermediates in their protein-folding catalytic pathway. To date, the bacteriophage encoded chaperonins ϕ-EL and OBP, human mitochondrial chaperonin and most recently, the bacterial groEL/ES systems, have been reported to form single-ring intermediates as part of their normal protein-folding activity. These double-ring chaperonins separate into single-ring intermediates that have the ability to independently fold a protein. We discuss the structural and functional features along with the biological relevance of single-ring intermediates in cellular protein folding. Of special interest are the ϕ-EL and OBP chaperonins which demonstrate features of both group I and II chaperonins in addition to their ability to function via single-ring intermediates.

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