naa a22 4500 510745814 CHVBK 20180411083045.0 cr unu---uuuuu 180411e20130101xx s 000 0 eng 10.1007/s12192-012-0360-4 doi (NATIONALLICENCE)springer-10.1007/s12192-012-0360-4 Probing the transient interaction between the small heat-shock protein Hsp21 and a model substrate protein using crosslinking mass spectrometry [Elektronische Daten] [Wietske Lambert, Gudrun Rutsdottir, Rasha Hussein, Katja Bernfur, Sven Kjellström, Cecilia Emanuelsson] Small heat-shock protein chaperones are important players in the protein quality control system of the cell, because they can immediately respond to partially unfolded proteins, thereby protecting the cell from harmful aggregates. The small heat-shock proteins can form large polydisperse oligomers that are exceptionally dynamic, which is implicated in their function of protecting substrate proteins from aggregation. Yet the mechanism of substrate recognition remains poorly understood, and little is known about what parts of the small heat-shock proteins interact with substrates and what parts of a partially unfolded substrate protein interact with the small heat-shock proteins. The transient nature of the interactions that prevent substrate aggregation rationalize probing this interaction by crosslinking mass spectrometry. Here, we used a workflow with lysine-specific crosslinking and offline nano-liquid chromatography matrix-assisted laser desorption/ionization tandem time-of-flight mass spectrometry to explore the interaction between the plant small heat-shock protein Hsp21 and a thermosensitive model substrate protein, malate dehydrogenase. The identified crosslinks point at an interaction between the disordered N-terminal region of Hsp21 and the C-terminal presumably unfolding part of the substrate protein. Cell Stress Society International, 2012 Lambert Wietske Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Institute for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, SE-221 00, Lund, Sweden aut Rutsdottir Gudrun Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Institute for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, SE-221 00, Lund, Sweden aut Hussein Rasha Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Institute for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, SE-221 00, Lund, Sweden aut Bernfur Katja Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Institute for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, SE-221 00, Lund, Sweden aut Kjellström Sven Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Institute for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, SE-221 00, Lund, Sweden aut Emanuelsson Cecilia Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Institute for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, SE-221 00, Lund, Sweden aut Cell Stress and Chaperones Springer Netherlands 18/1(2013-01-01), 75-85 1355-8145 18:1<75 2013 18 12192 https://doi.org/10.1007/s12192-012-0360-4 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s12192-012-0360-4 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Lambert Wietske Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Institute for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, SE-221 00, Lund, Sweden aut NATIONALLICENCE 700 1- Rutsdottir Gudrun Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Institute for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, SE-221 00, Lund, Sweden aut NATIONALLICENCE 700 1- Hussein Rasha Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Institute for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, SE-221 00, Lund, Sweden aut NATIONALLICENCE 700 1- Bernfur Katja Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Institute for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, SE-221 00, Lund, Sweden aut NATIONALLICENCE 700 1- Kjellström Sven Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Institute for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, SE-221 00, Lund, Sweden aut NATIONALLICENCE 700 1- Emanuelsson Cecilia Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Institute for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, SE-221 00, Lund, Sweden aut NATIONALLICENCE 773 0- Cell Stress and Chaperones Springer Netherlands 18/1(2013-01-01), 75-85 1355-8145 18:1<75 2013 18 12192 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer