Escherichia coli small heat shock protein IbpA plays a role in regulating the heat shock response by controlling the translation of σ³².

ABSTRACT: Small heat shock proteins (sHsps) act as ATP-independent chaperones that prevent irreversible aggregate formation by sequestering denatured proteins. IbpA, an Escherichia coli sHsp, functions not only as a chaperone but also as a suppressor of its own expression through posttranscriptional regulation, contributing to negative feedback regulation. IbpA also regulates the expression of its paralog, IbpB, in a similar manner, but the extent to which IbpA regulates other protein expressions is unclear. We have identified that IbpA down-regulates the expression of many Hsps by repressing the translation of the heat shock transcription factor σ³². The IbpA regulation not only controls the σ³² level but also contributes to the shutoff of the heat shock response. These

SUBMITTER: Miwa T 

PROVIDER: S-EPMC10410725 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature