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

Ewelina M Krysztofinska; Nicola J Evans; Arjun Thapaliya; James W Murray; Rhodri M L Morgan; Santiago Martinez-Lumbreras; Rivka L Isaacson

doi:10.3389/fmolb.2017.00068

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

Ewelina M Krysztofinska, Nicola J Evans, Arjun Thapaliya, James W Murray, Rhodri M L Morgan, Santiago Martinez-Lumbreras, Rivka L Isaacson

Chemistry

Research output: Contribution to journal › Article › peer-review

17 Citations (Scopus)

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.

Original language	English
Pages (from-to)	68
Journal	Frontiers in Molecular Biosciences
Volume	4
DOIs	https://doi.org/10.3389/fmolb.2017.00068
Publication status	Published - 11 Oct 2017

Keywords

Journal Article

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10.3389/fmolb.2017.00068

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AU - Krysztofinska, Ewelina M

AU - Evans, Nicola J

AU - Thapaliya, Arjun

AU - Murray, James W

AU - Morgan, Rhodri M L

AU - Martinez-Lumbreras, Santiago

AU - Isaacson, Rivka L

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AB - 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.

KW - Journal Article

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DO - 10.3389/fmolb.2017.00068

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JF - Frontiers in Molecular Biosciences

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

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