Coevolution analyses illuminate the dependencies between amino acid sites in the chaperonin system GroES-L.

ABSTRACT:

Background

GroESL is a heat-shock protein ubiquitous in bacteria and eukaryotic organelles. This evolutionarily conserved protein is involved in the folding of a wide variety of other proteins in the cytosol, being essential to the cell. The folding activity proceeds through strong conformational changes mediated by the co-chaperonin GroES and ATP. Functions alternative to folding have been previously described for GroEL in different bacterial groups, supporting enormous functional and structural plasticity for this molecule and the existence of a hidden combinatorial code in the protein sequence enabling such functions. Describing this plasticity can shed light on the functional diversity of GroEL. We hypothesize that different overlapping sets of amino acids coevolve within GroEL

SUBMITTER: Ruiz-Gonzalez MX 

PROVIDER: S-EPMC3728108 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature