Abstract
The discovery of heat shock proteins shaped our view of protein folding in the cell. Since their initial discovery, chaperone proteins were identified in all domains of life, demonstrating their vital and conserved functional roles in protein homeostasis. Chaperone proteins maintain proper protein folding in the cell by utilizing a variety of distinct, characteristic mechanisms to prevent aberrant intermolecular interactions, prevent protein aggregation, and lower entropic costs to allow for protein refolding. Continued study has found that chaperones may exhibit alternative functions, including maintaining protein folding during endoplasmic reticulum (ER) import and chaperone-mediated degradation, among others. Alternative chaperone functions are frequently controlled by post-translational modification, in which a given chaperone can switch between functions through covalent modification. This review will focus on the Hsp70 class chaperones and their Hsp40 co-chaperones, specifically highlighting the importance of post-translational control of chaperones. These modifications may serve as a target for therapeutic intervention in the treatment of diseases of protein misfolding and aggregation.
Highlights
The discovery of heat shock proteins shaped our view of protein folding in the cell
Since the residues of amino acid side chains differ in size, charge, and polarity, each amino acid offers an incredible amount of biochemical diversity that defines the subsequent structure and function of each respective protein after translation and folding
While the amino acid sequence of a protein cannot be altered post-translationally, the chemistry of specific amino side chains can be altered through a collection of post-translational modifications (PTMs)
Summary
All proteins consist of specific combinations of twenty different amino acids. Since the residues of amino acid side chains differ in size, charge, and polarity, each amino acid offers an incredible amount of biochemical diversity that defines the subsequent structure and function of each respective protein after translation and folding. While the amino acid sequence of a protein cannot be altered post-translationally, the chemistry of specific amino side chains can be altered through a collection of post-translational modifications (PTMs). PTMs occur in response to changing cellular environments and are catalyzed on specific residues of target proteins by a collection of specialized enzymes. These enzymes are part of a greater network of cell communication pathways to allow for the immediate response to altered cellular conditions. Methylation and acetylation typically occurs at lysine residues, acting to neutralize the residue while adding large steric constraints [3,4] Larger macromolecules such as carbohydrates and lipids may be used to modify proteins. This review will focus on the post-translational modification of Hsp class chaperones as well as their interacting co-chaperones
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