Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding

Sophia Ungelenk, Fatemeh Moayed, Chi-Ting Ho, Tomas Grousl, Annette Scharf, Alireza Mashaghi, Sander Tans, Matthias P. Mayer (), Axel Mogk () and Bernd Bukau ()
Additional contact information
Sophia Ungelenk: Center for Molecular Biology of the University of Heidelberg (ZMBH), DKFZ-ZMBH Alliance
Fatemeh Moayed: FOM Institute for Atomic and Molecular Physics (AMOLF)
Chi-Ting Ho: Center for Molecular Biology of the University of Heidelberg (ZMBH), DKFZ-ZMBH Alliance
Tomas Grousl: Center for Molecular Biology of the University of Heidelberg (ZMBH), DKFZ-ZMBH Alliance
Annette Scharf: Center for Molecular Biology of the University of Heidelberg (ZMBH), DKFZ-ZMBH Alliance
Alireza Mashaghi: FOM Institute for Atomic and Molecular Physics (AMOLF)
Sander Tans: FOM Institute for Atomic and Molecular Physics (AMOLF)
Matthias P. Mayer: Center for Molecular Biology of the University of Heidelberg (ZMBH), DKFZ-ZMBH Alliance
Axel Mogk: Center for Molecular Biology of the University of Heidelberg (ZMBH), DKFZ-ZMBH Alliance
Bernd Bukau: Center for Molecular Biology of the University of Heidelberg (ZMBH), DKFZ-ZMBH Alliance

Nature Communications, 2016, vol. 7, issue 1, 1-14

Abstract: Abstract Small heat shock proteins (sHsp) constitute an evolutionary conserved yet diverse family of chaperones acting as first line of defence against proteotoxic stress. sHsps coaggregate with misfolded proteins but the molecular basis and functional implications of these interactions, as well as potential sHsp specific differences, are poorly explored. In a comparative analysis of the two yeast sHsps, Hsp26 and Hsp42, we show in vitro that model substrates retain near-native state and are kept physically separated when complexed with either sHsp, while being completely unfolded when aggregated without sHsps. Hsp42 acts as aggregase to promote protein aggregation and specifically ensures cellular fitness during heat stress. Hsp26 in contrast lacks aggregase function but is superior in facilitating Hsp70/Hsp100-dependent post-stress refolding. Our findings indicate the sHsps of a cell functionally diversify in stress defence, but share the working principle to promote sequestration of misfolding proteins for storage in native-like conformation.

Date: 2016
References: Add references at CitEc
Citations: View citations in EconPapers (3)

Downloads: (external link)
https://www.nature.com/articles/ncomms13673 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13673

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms13673

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().