Principle of protein folding in the cellular environment

Principle of protein folding in the cellular environment

Principle of protein folding in the cellular environment The ability of newly synthesized protein chains to fold into their functional form within the complex intracellular environment. Molecular Chaperons Proteins that help the folding of other proteins, usually through

cycles of binding and release, without forming part of their final native structure. Increase in the efficiency, not the specificity, of protein folding Change in emphasis from post-translational modification to cotranslational modification In vitro, both GroEL and Hsp70 interact promiscuously with most unfolded proteins. Protein folding in the cytosol of

prokaryotic and eukaryotic cells. TF: Trigger Factor NAC: nascent-chain associated complex Folding of small protein Hsp 70 and chaperonin

independent Folding of aggregation sensitive or multidomain small chaperon dependent (e.g. Hsp 70 or TF Folding of complex proteins with discontinuous surfaces:

chaperons dependent ATPase Cycle and Atomic Structure of the ATPase Domain of Hsp70 Proteins A chaperonin called GroEL-GroES complex (from Escherichia coli)

Two rings of 7x2GroEL proteins (shown in blue and green) with a cap (just on one side) of GroES proteins (red and yellow) Pathways of chaperone-mediated protein folding in the cytosol Nascent polypeptide chains are met by trigger factor (TF) as they emerge from the ribosome.

The 70-kDa heat-shock protein DnaK, which is stimulated by its J-domain co-chaperone DnaJ, also binds synthesized

nascent polypeptides. polypeptides can

Newly fold spontaneously or can be assisted by DnaK. Alternatively, they can be passed to the GroEL GroES chaperonin system for final folding, and, in some cases, might again interact with DnaK.

The steric information necessary for newly synthesized protein chains to fold correctly within cells resides solely in the primary structure of the initial translation product. Three families of molecular chaperone best known to interact with newly synthesized protein: hsp70, hsp40, and chaperonins

Reference

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