title: Oligomer-dependent and -independent chaperone activity of sHsps in different stressed conditions.
abstract: A great number of studies have proven that sHsps protect cells by inhibiting protein aggregation under heat stress, while little is known about their function to protect cells under acid stress. In this work, we show that Hsp20.1 and Hsp14.1 oligomers dissociated to smaller oligomeric species or even dimer/monomer at low pH (pH 4.0 and pH 2.0), whereas no prominent quaternary structural changes were seen at 50 °C. Both oligomers and smaller oligomeric species exhibited abilities to suppress client aggregation at low pH and at 50 °C. These results suggest that sHsps may function in different modes in different stressed conditions.
authors.affiliation: School of Bioscience and Bioengineering, South China University of Technology, Guangzhou 510006, China.
authors.forename: Liang
authors.initials: L
authors.lastname: Liu
authors.affiliation: Institute of Systems Biomedicine and Department of Biophysics, School of Basic Medical Sciences, Peking University Health Science Center, Beijing 100191, China.
authors.forename: Jiyun
authors.initials: J
authors.lastname: Chen
authors.affiliation: School of Bioscience and Bioengineering, South China University of Technology, Guangzhou 510006, China.
authors.forename: Bo
authors.initials: B
authors.lastname: Yang
authors.affiliation: College of Light Industry and Food Sciences, South China University of Technology, Guangzhou 510641, China.
authors.forename: Yonghua
authors.initials: Y
authors.lastname: Wang
keywords: Acid stress; CTE, C-terminal extension; EM, electron microscopy; Hsp14.0, Sulfolobus tokodaii heat shock protein 14.0; Hsp14.1, Sulfolobus solfataricus heat shock 14.1; Hsp20.1, Sulfolobus solfataricus heat shock 20.1; MDH, malate dehydrogenase; Molecular chaperone; SEC, size exclusion chromatography; Small heat shock protein (sHsp); Temperature stress; sHsps, small heat shock proteins
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