Team:UNC-Asheville/BasicParts

Basic Parts

Chaperone Proteins are the proteins for you and me.

GroEL/ES
Chaperone Protein

Description

GroEl/Es is a chaperone protein complex present in many bacteria including E.coli. Gro El encodes a barrel-like structure and requires the “lid” protein GroEs to function properly. Unfolded proteins bind to a hydrophobic patch near the inner lip of GroEL, inducing GroEs to bind. This patch is then “hidden” in a conformational change, exposing the protein to the hydrophilic environment of the protein interior. In the tight space, the entropic cost of protein folding is lowered and proteins will fold and unfold repeatedly until reaching the native structure. The protein is then released into the cytoplasm.

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History

Although this protein is naturally encoded by E.coli, it was demonstrated by the Braunschweig 2014 iGEM team that using the GroEl/Es plasmid from the Takara Chaperone protein kit allowed for the six subunits of sMMO to assemble properly. Rather than spend the money on the kit, our team decided to make GroEl/Es a Biobrick. Future work with this part will attempt to put it under the inducible pBAD promoter for tight expression with arabinose. The coding sequence was pulled from K12 E.coli and edited to remove 6 restriction sites which were not Biobrick compatible while retaining amino acid sequence and noting codon usage.

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