Cyanobacteria constitute a heterogeneous phylum of oxygen-producing, photosynthetic prokaryotes. They are susceptible to various stress conditions like heat, salt, or light stress, all inducing the cyanobacterial heat shock response (HSR). Cyanobacterial small heat shock proteins (sHsps) are known to preserve thylakoid membrane integrity under stress conditions, thereby protecting the photosynt...

Small heat shock proteins (sHSPs) are ubiquitous chaperones that bind and sequester non-native proteins preventing their aggregation. Despite extensive studies of sHSPs chaperone activity, the location of the bound substrate within the sHSP oligomer has not been determined. In this paper, we used cryoelectron microscopy (cryoEM) to visualize destabilized mutants of T4 lysozyme (T4L) bound to en...

Carotenoid-protein complex (CPC) was isolated from chromoplast-enriched suspensions of cassava storage root (CSR) using size exclusion chromatography and characterized. Peptide sequences (LC_MS/MS spectrum) obtained from CPC and their corresponding proteins were obtained using publically available databases. Small Heat Shock Proteins (sHSPs) were the most abundant proteins identified in the CPC...

The small heat shock proteins (sHSPs) and alpha-crystallins are highly effective, ATP-independent chaperones that can bind denaturing client proteins to prevent their irreversible aggregation. One model of sHSP function suggests that the oligomeric sHSPs are activated to the client-binding form by dissociation at elevated temperatures to dimers or other sub-oligomeric species. Here we examine t...

Historically, small heat shock proteins (sHSPs) have been extensively studied in the context of being intracellular molecular chaperones. However, recent studies looking at the role of sHSPs in neurological diseases have demonstrated a near universal upregulation of certain sHSPs in damaged and diseased brains. Initially, it was thought that sHSPs are pathological in these disease states becaus...

Small heat shock proteins (sHSPs) perform a fundamental role in protecting cells against a wide array of stresses but their biological function during viral infection remains unknown. Rice stripe virus (RSV) causes a severe disease of rice in Eastern Asia. OsHSP20 and its homologue (NbHSP20) were used as baits in yeast two-hybrid (YTH) assays to screen an RSV cDNA library and were found to inte...

Small heat shock proteins (sHSPs) are oligomeric stress proteins characterized by an α-crystallin domain (ACD) surrounded by a N-terminal arm and C-terminal extension. Publications on sHSPs have reported that they exist in prokaryotes and eukaryotes but, to our knowledge, not in viruses. Here we show that sHSPs are present in some cyanophages that infect the marine unicellular cyanobacteria, Sy...

A broad survey of most of the major geyser basins within Yellowstone National Park (Wyoming, USA) was conducted to identify the flowering plants which tolerate high rhizosphere temperatures (> or = 40 degrees C) in geothermally heated environments. Under such conditions, five species of monocots and four species of dicots were repeatedly found. The predominant flowering plants in hot soils (>40...

BACKGROUND αB-crystallin and HSP27 are mammalian intracellular small heat shock proteins. RESULTS These proteins exchange subunits in a rapid and temperature-dependent manner. CONCLUSION This facile subunit exchange suggests that differential expression could be used by the cell to regulate the response to stress. SIGNIFICANCE A robust technique defines parameters for the dynamic interact...

Small heat-shock proteins (sHSPs) are ubiquitous ATP-independent molecular chaperones that play crucial roles in protein quality control in cells. They are able to prevent the aggregation and/or inactivation of various non-native substrate proteins and assist the refolding of these substrates independently or under the help of other ATP-dependent chaperones. Substrate recognition and binding by...