Structure and Interactions of the TPR Domain of Sgt2 with Yeast Chaperones and Ybr137wp.

Frontiers in Molecular Biosciences
Ewelina M KrysztofinskaRivka L Isaacson

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.

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Citations

May 24, 2019·The Biochemical Journal·Marie-Eve ChagotMarc Quinternet
May 29, 2018·Cell Stress & Chaperones·Tambudzai KudzeAmie J McClellan
Nov 18, 2019·Biophysics Reviews·Thiago V SeraphimWalid A Houry
Jun 17, 2019·The Protein Journal·Nica BorgeseBlanche Schwappach
Oct 3, 2019·The Journal of Biological Chemistry·Shu-Ou Shan
Jul 16, 2021·The Journal of Cell Biology·Ákos Farkas, Katherine E Bohnsack

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Methods Mentioned

BETA
X-ray
isothermal
Nuclear magnetic resonance
NMR
PCR

Software Mentioned

PHENIX
NMRPipe
REFMAC5
Aimless
SLEEDLNLD
MEEVD
ccp4mg
MicroCal
PyMOL
PTVEEVD

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