Small heat shock proteins are a diverse, ancient, and important family of proteins. All organisms possess small heat shock proteins (sHSPs), indicating that these proteins evolved very early in the history of life prior to the divergence of the three domains of life (Archaea, Bacteria, and Eukarya). Comparing the structures of sHSPs from diverse organisms across these three domains reveals that...

Small heat shock proteins (sHsp) constitute an evolutionary conserved yet diverse family of chaperones acting as first line of defence against proteotoxic stress. sHsps coaggregate with misfolded proteins but the molecular basis and functional implications of these interactions, as well as potential sHsp specific differences, are poorly explored. In a comparative analysis of the two yeast sHsps...

The timing and tissue localization of small heat shock proteins (sHSPs) during cork oak somatic embryo development was investigated under normal growing culture conditions and in response to stress. Western blot analyses using polyclonal antibodies raised against cork oak recombinant HSP17 showed a transient accumulation of class I sHSPs during somatic embryo maturation and germination. Moreove...

Small heat shock proteins (sHSPs), as ubiquitous molecular chaperones found in all forms of life, are known to be able to protect cells against stresses and suppress the aggregation of a variety of model substrate proteins under in vitro conditions. Nevertheless, it is poorly understood what natural substrate proteins are protected by sHSPs in living cells. Here, by using a genetically incorpor...

The ever-increasing num ber of proteins Introduction identified as belonging to the family of small heat-shock proteins (shsps) and a-crystallins enables us to reassess The small heat-shock proteins (shsps) are one of the four the phylogeny of this ubiquitous protein family. While most common groups of heat-shock proteins (Lindquist the prokaryotic and fungal representatives are not prop­ erly ...

Higher plants; Crop plants; Chaperones; Heat-shock proteins; Transcription factors; Stress; Heat stress; Heat tolerance Abstract Plants as sessile organisms are exposed to persistently changing stress factors. The primary stresses such as drought, salinity, cold and hot temperatures and chemicals are interconnected in their effects on plants. These factors cause damage to the plant cell and lea...

The results of this study describe the identification and characterization of the Toxoplasma gondii alpha-crystallin/small heat shock protein (sHsp) family. By database (www.toxodb.org) search, five parasite sHsps (Hsp20, Hsp21, Hsp28, Hsp29, and the previously characterized Hsp30/Bag1) were identified. As expected, they share the homologous alpha-crystallin domain, which is the key characteris...

The ubiquitous small heat shock proteins (sHSPs) are well documented to act in vitro as molecular chaperones to prevent the irreversible aggregation of heat-sensitive proteins. However, the in vivo activities of sHSPs remain unclear. To investigate the two most abundant classes of plant cytosolic sHSPs (class I [CI] and class II [CII]), RNA interference (RNAi) and overexpression lines were crea...

The small heat-shock proteins (sHSPs) comprise a family of molecular chaperones which are widespread but poorly understood. Despite considerable effort, comparatively few high-resolution structures have been determined for the sHSPs, a likely consequence of their tendency to populate ensembles of inter-converting conformational and oligomeric states at equilibrium. This dynamic structure appear...

Small heat shock proteins (sHsps) are a conserved protein family, with members found in all organisms analysed so far. Several sHsps have been shown to exhibit chaperone activity and protect proteins from irreversible aggregation in vitro. Here we show that Hsp26, an sHsp from Saccharomyces cerevisiae, is a temperature-regulated molecular chaperone. Like other sHsps, Hsp26 forms large oligomeri...