Small but mighty: a functional look at bacterial sHSPs

Abstract

Small heat shock proteins (sHSPs) are widespread in every kingdom of life, being indispensable for protein quality control networks. Alongside canonical chaperone functions, sHSPs seem to have been a very plastic scaffold for acquiring multiple related functions across evolution. This review aims to summarize what is known about sHSPs functioning in the Bacteria Kingdom.

Genome-Wide Assessment of Stress-Associated Genes in Bifidobacteria

“…Rather, Hsp20 may be important for coping with stressors other than heat, as suggested before ( 30 ). In other organisms, small heat shock proteins, such as Hsp20, have been linked to functions other than classical chaperones, e.g., biofilm formation and cell protection during dormancy ( 55 ). Interestingly, animal isolates have been shown to commonly grow at higher temperatures than human isolates (up to 45°C) ( 56 ).…”

Blowing Hot and Cold: Body Temperature and the Microbiome

“…The heat shock response is a conserved regulatory network found in all branches in life. Heat shock proteins include chaperones that stabilize and refold denatured proteins, and ATP-dependent proteases that degrade the misfolded proteins ( 5 , 6 ). The complementary cold shock response is characterized by nucleic acid chaperones that prevent the formation of secondary structures in mRNA ( 7 ).…”

Molecular chaperone function of three small heat-shock proteins from a model probiotic species

“…Although bacterial sHSP have been thoroughly studied (Obuchowski and Liberek 2020;Obuchowski et al 2021), chiefly in model species such as E. coli (Piróg et al 2021), only a very few works have investigated the sHSP of probiotic microorganisms (Capozzi et al 2011b;Khaskheli et al 2015). The involvement of L. plantarum sHSP in stress response strategies was demonstrated previously, mainly by expression, gene knockout (KO) and phenotypic studies (Fiocco et al 2007;Capozzi et al 2011a;Arena et al 2019).…”