Escherichia coli small heat shock protein IbpA plays a role in regulating the heat shock response by controlling the translation of σ 32
2023; National Academy of Sciences; Volume: 120; Issue: 32 Linguagem: Inglês
10.1073/pnas.2304841120
ISSN1091-6490
Autores Tópico(s)Protein Structure and Dynamics
ResumoSmall 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 σ 32 . The IbpA regulation not only controls the σ 32 level but also contributes to the shutoff of the heat shock response. These results revealed an unexplored role of IbpA to regulate heat shock response at a translational level, which adds an alternative layer for tightly controlled and rapid expression of σ 32 on demand.
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