A special type of molecular chaperone proteins, so called small heat shock protein (sHsp) chaperones, are investigated. The sHsps are multimeric proteins which are crucial to promote survival of cells. The sHsps act through interaction with early unfolding intermediates of other proteins and prevent their aggregation. The sHsps are ubiquitously expressed, with 10 different homologues in the human genome and 25 different homologues in Arabidopsis thaliana. We have found that overexpression of Hsp21, a chloroplast localized sHsp, increases plant stress resistance and we have characterized recombinantly expressed Hsp21.
We investigate protein-protein interactions to elucidate the mechanism of how sHsps interact with and protect cellular client proteins, by chemical crosslinking, mass spectrometric mapping of crosslinked peptides, single particle EM and NMR.
Ulrika Härndahl, PhD thesis, Lund University, 2000
Niklas Gustavsson, PhD thesis, Lund University, 2001
Emma Åhrman, PhD thesis, Lund University, 2007
Wietske Lambert, PhD thesis, Lund University, 2012
Gudrun Rutsdottir, PhD thesis, Lund University, 2017