A Study on the Temperature-Dependent Behavior of Small Heat Shock Proteins from Methanogens.

ABSTRACT: Small heat shock proteins (sHsps) are ubiquitous low-molecular-weight chaperones that prevent protein aggregation under cellular stress conditions. In the absence of stress, they assemble into large oligomers. In response to stress, such as elevated temperatures, they undergo conformational changes that expose hydrophobic surfaces, allowing them to interact with denatured proteins. At heat shock temperatures in bacteria, large sHsp oligomers disassemble into smaller oligomeric forms. Methanogens are a diverse group of microorganisms, ranging from thermophilic to psychrophilic and halophilic species. Accordingly, their sHsps exhibit markedly different temperature dependencies based on their optimal growth temperatures. In this study, we characterized sHsps from both hyperthermophilic and me

SUBMITTER: Kurokawa N 

PROVIDER: S-EPMC12193508 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature