AUTHOR=Krysztofinska Ewelina M. , Evans Nicola J. , Thapaliya Arjun , Murray James W. , Morgan Rhodri M. L. , Martinez-Lumbreras Santiago , Isaacson Rivka L. TITLE=Structure and Interactions of the TPR Domain of Sgt2 with Yeast Chaperones and Ybr137wp JOURNAL=Frontiers in Molecular Biosciences VOLUME=4 YEAR=2017 URL=https://www.frontiersin.org/journals/molecular-biosciences/articles/10.3389/fmolb.2017.00068 DOI=10.3389/fmolb.2017.00068 ISSN=2296-889X ABSTRACT=

Small glutamine-rich tetratricopeptide repeat-containing protein 2 (Sgt2) is a multi-module co-chaperone involved in several protein quality control pathways. The TPR domain of Sgt2 and several other proteins, including SGTA, Hop, and CHIP, is a highly conserved motif known to form transient complexes with molecular chaperones such as Hsp70 and Hsp90. In this work, we present the first high resolution crystal structures of Sgt2_TPR alone and in complex with a C-terminal peptide PTVEEVD from heat shock protein, Ssa1. Using nuclear magnetic resonance spectroscopy and isothermal titration calorimetry, we demonstrate that Sgt2_TPR interacts with peptides corresponding to the C-termini of Ssa1, Hsc82, and Ybr137wp with similar binding modes and affinities.