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The preferential heterodimerization of human small heat shock proteins HSPB1 and HSPB6 is dictated by the N-terminal domain.
Heirbaut, Michelle; Lermyte, Frederik; Martin, Esther M; Beelen, Steven; Verschueren, Tim; Sobott, Frank; Strelkov, Sergei V; Weeks, Stephen D.
Afiliación
  • Heirbaut M; Laboratory for Biocrystallography, Dept. of Pharmaceutical and Pharmacological Sciences, KU Leuven, Belgium.
  • Lermyte F; Biomolecular and Analytical Mass Spectrometry Group, Dept. of Chemistry, University of Antwerp, Belgium; Centre for Proteomics, University of Antwerp, Belgium.
  • Martin EM; Biomolecular and Analytical Mass Spectrometry Group, Dept. of Chemistry, University of Antwerp, Belgium.
  • Beelen S; Laboratory for Biocrystallography, Dept. of Pharmaceutical and Pharmacological Sciences, KU Leuven, Belgium.
  • Verschueren T; Biomolecular and Analytical Mass Spectrometry Group, Dept. of Chemistry, University of Antwerp, Belgium.
  • Sobott F; Biomolecular and Analytical Mass Spectrometry Group, Dept. of Chemistry, University of Antwerp, Belgium.
  • Strelkov SV; Laboratory for Biocrystallography, Dept. of Pharmaceutical and Pharmacological Sciences, KU Leuven, Belgium. Electronic address: sergei.strelkov@kuleuven.be.
  • Weeks SD; Laboratory for Biocrystallography, Dept. of Pharmaceutical and Pharmacological Sciences, KU Leuven, Belgium. Electronic address: stephen.weeks@kuleuven.be.
Arch Biochem Biophys ; 610: 41-50, 2016 Nov 15.
Article en En | MEDLINE | ID: mdl-27717639
Small heat shock proteins are ATP-independent molecular chaperones. Their function is to bind partially unfolded proteins under stress conditions. In vivo, members of this chaperone family are known to preferentially assemble together forming large, polydisperse heterooligomers. The exact molecular mechanisms that drive specific heteroassociation are currently unknown. Here we study the oligomers formed between human HSPB1 and HSPB6. Using small-angle X-ray scattering we could characterize two distinct heterooligomeric species present in solution. By employing native mass spectrometry we show that such assemblies are formed purely from heterodimeric building blocks, in line with earlier cross-linking studies. Crucially, a detailed analysis of truncation variants reveals that the preferential association between these two sHSPs is solely mediated by their disordered N-terminal domains.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas del Choque Térmico HSP20 / Proteínas de Choque Térmico HSP27 Límite: Humans Idioma: En Revista: Arch Biochem Biophys Año: 2016 Tipo del documento: Article País de afiliación: Bélgica Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas del Choque Térmico HSP20 / Proteínas de Choque Térmico HSP27 Límite: Humans Idioma: En Revista: Arch Biochem Biophys Año: 2016 Tipo del documento: Article País de afiliación: Bélgica Pais de publicación: Estados Unidos