The small heat-shock proteins HSPB2 and HSPB3 form well-defined heterooligomers in a unique 3 to 1 subunit ratio.

Journal article

Various mammalian small heat-shock proteins (sHSPs) can interact with one another to form large polydisperse assemblies. In muscle cells, HSPB2/MKBP (myotonic dystrophy protein kinase-binding protein) and HSPB3 have been shown to form an independent complex. To date, the biochemical properties of this complex have not been thoroughly characterized. In this study, we show that recombinant HSPB2 and HSPB3 can be successfully purified from Escherichia coli cells co-expressing both proteins. Nano...

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Authors: den Engelsman, J; Boros, S; Dankers, P; Kamps, B; Vree Egberts, W

• Publication status: Published
• Journal: Journal of molecular biology
• Volume: 393
• Issue: 5
• Pages: 1022-1032
• Publication date: 2009-11-01
• DOI: 10.1016/j.jmb.2009.08.052
• EISSN: 1089-8638
• ISSN: 0022-2836
• Language: English
• Keywords: Protein Structure, Quaternary; Hydrophobic and Hydrophilic Interactions; Rats; Anilino Naphthalenesulfonates; Molecular Sequence Data; Humans; Protein Binding; Spectrometry, Mass, Electrospray Ionization; Hot Temperature; Circular Dichroism; Molecular Weight; Heat-Shock Proteins; Surface Properties; Amino Acid Sequence; Animals; Protein Subunits; HSP27 Heat-Shock Proteins; Sequence Alignment