Quantification of interaction strengths between chaperones and tetratricopeptide repeat domain-containing membrane proteins

Abstract

Background: Tetratricopeptide repeat proteins at organellar surfaces serve as docking proteins for chaperone-bound preproteins. Results: Binding affinities of docking proteins and chaperones were determined using surface plasmon resonance spectroscopy, Interaction Map® analysis, and microscale thermophoresis. Conclusion: Docking proteins of the chloroplast, mitochondrion, and endoplasmic reticulum bind differentially to various cytosolic chaperones. Significance: Tetratricopeptide repeat docking proteins possibly discriminate between chaperones in the cytosol. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.