The oligomeric plasticity of Hsp20 of Sulfolobus acidocaldarius protects environment-induced protein aggregation and membrane destabilization.
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Hsp20 exists as a ~24-mer at room temperature and forms higher oligomeric forms at higher temperature (50-70 degrees C) and lower pH (3.0-5.0).
"Our data suggested the existence of a ~24-mer of Hsp20 at room temperature (25 °C) and a higher oligomeric form at higher temperature (50 °C-70 °C) and lower pH (3.0-5.0)"
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The dimer is the functional conformation in the presence of aggregating substrate proteins.
"we identified a dimeric form of protein as the functional conformation in the presence of aggregating substrate proteins"
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Hsp20 protects against stress-induced protein aggregation.
"it plays a key role in the protection of stress-induced protein aggregation"
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Hsp20 interacts with membrane lipids via hydrophobic interaction and stabilizes membranes.
"Hsp20 interacts with membrane lipids via a hydrophobic interaction and it lowers the propensity of in vitro phase transition of bacterial and archaeal lipids"
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Hsp20 has been found in secretory vesicles despite being a non-secreted protein.
"Hsp20, despite being a non-secreted protein, has been reported to be present in secretory vesicles"