Hsp20 is a member of the small heat shock superfamily of proteins that function as chaperones to prevent protein misfolding through adenosine triphosphate−independent processes. It is widely expressed but is
Archaeal sHsps are thus by far the least explored among the molecular chaperones. In general, representatives of the third domain of life, archaea, are a highly diverse and abundant group of organisms including many ‘extremophiles’ that thrive in harsh environments like salt lakes, hot solfatari...
Hsp20s function as ATP-independent molecular chaperones and accumulate in order to protect plants by preventing protein aggregation and facilitating refolding of damaged proteins under heat stress conditions [20]. They may participate in heat tolerance through pathways dependent on heat shock transcription...
Hsp20s are ATP-independent molecular chaperones and can form oligomeric protein complexes of 200–800 kDa, which consist of 9 to 50 subunits [14, 15]. Hsp20 can avert protein denaturation, and thus maintain the stability and normal functions of proteins in both eukaryotic and prokaryotic cells...