Chaperone-client interactions between Hsp21 and client proteins monitored in solution by small angle X-ray scattering and captured by crosslinking mass spectrometry

Proteins
Gudrun RutsdottirChristopher A G Söderberg

Abstract

The small heat shock protein (sHsp) chaperones are important for stress survival, yet the molecular details of how they interact with client proteins are not understood. All sHsps share a folded middle domain to which is appended flexible N- and C-terminal regions varying in length and sequence between different sHsps which, in different ways for different sHsps, mediate recognition of client proteins. In plants there is a chloroplast-localized sHsp, Hsp21, and a structural model suggests that Hsp21 has a dodecameric arrangement with six N-terminal arms located on the outside of the dodecamer and six inwardly-facing. Here, we investigated the interactions between Hsp21 and thermosensitive model substrate client proteins in solution, by small-angle X-ray scattering (SAXS) and crosslinking mass spectrometry. The chaperone-client complexes were monitored and the Rg -values were found to increase continuously during 20 min at 45°, which could reflect binding of partially unfolded clients to the flexible N-terminal arms of the Hsp21 dodecamer. No such increase in Rg -values was observed with a mutational variant of Hsp21, which is mainly dimeric and has reduced chaperone activity. Crosslinking data suggest that the chaperone-client ...Continue Reading

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Citations

Apr 17, 2020·The New Phytologist·Elizabeth R Waters, Elizabeth Vierling
Feb 10, 2019·Nature Communications·Filipa TeixeiraUrsula Jakob
Nov 24, 2019·Biophysical Journal·Fatemeh MoayedSander J Tans
May 23, 2021·Nature Communications·Chuanyang YuWilson Chun Yu Lau
Jan 22, 2022·FEBS Letters·Sibel UzunçayırKarin Lindkvist-Petersson

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