Journal article
The Monomeric α-Crystallin Domain of the Small Heat-shock Proteins αB-crystallin and Hsp27 Binds Amyloid Fibril Ends
Emily E Selig, Roberta J Lynn, Courtney O Zlatic, Yee-Foong Mok, Heath Ecroyd, Paul R Gooley, Michael DW Griffin
JOURNAL OF MOLECULAR BIOLOGY | ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD | Published : 2022
Abstract
Small heat-shock proteins (sHSPs) are ubiquitously expressed molecular chaperones present in all kingdoms of life that inhibit protein misfolding and aggregation. Despite their importance in proteostasis, the structure–function relationships of sHSPs remain elusive. Human sHSPs are characterised by a central, highly conserved α-crystallin domain (ACD) and variable-length N- and C-terminal regions. The ACD forms antiparallel homodimers via an extended β-strand, creating a shared β-sheet at the dimer interface. The N- and C-terminal regions mediate formation of higher order oligomers that are thought to act as storage forms for chaperone-active dimers. We investigated the interactions of the A..
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Awarded by Australian Research Council Future Fellowship
Funding Acknowledgements
E.E.S is a recipient of an Australian Government Research Training Program Scholarship. M.D.W.G is the recipient of an Australian Research Council Future Fellowship (project number FT140100544) . We thank Shenggen Yao for assistance with collection of NMR spectra. We also acknowledge the Melbourne Magnetic Resonance Facility, the Melbourne Protein Characterisation Platform, the Ian Holmes Imaging Centre, and the Melbourne Mass Spectrometry and Proteomics Facility, at the Bio21 Molecular Science and Biotechnology Institute, for technical support.