The Escherichia coli small heat shock protein IbpA plays a role in regulating the heat shock response by controlling the translation of σ32
The Escherichia coli small heat shock protein IbpA plays a role in regulating the heat shock response by controlling the translation of σ32
复制标题
大肠杆菌小热激蛋白IbpA通过控制σ32的翻译来发挥调节热激反应的作用
DOI:
10.1101/2023.03.28.534623
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发表时间:
2023
期刊:
影响因子:
--
通讯作者:
Hideki Taguchi
中科院分区:
文献类型:
--
作者:
Tsukumi Miwa; Hideki Taguchi
Heat Shock Proteins. IbpA regulates the expression of itself and its paralog, ibpB, at the posttranscriptional level (28). The stem loops present in the 5′ UTR of the mRNA of ibpAor ibpBconstitute a key regulatory element. While secondary structures with multiple stemloops are common in the 5′ UTRs of ibpA and ibpB, their sequences and structures are not identical (26, 27). Therefore, we hypothesized that, apart from self-regulation, IbpA may also influence the expression of other proteins in E. coli. To identify potential targets of IbpA-mediated regulation, we conducted a mass spectrometry (MS)–based quantitative proteomics analysis to identify proteins, whose expression is altered in E. coli upon IbpA overexpression. We compared the proteomes of cells overexpressing IbpA and those overexpressing GFP as a control and found that 41 and 40 proteins were specifically increased (> 1.67-fold) and decreased (< 0.6-fold), respectively, upon IbpA overexpression (Fig. 1A and Dataset S1). Gene ontology (GO) analysis revealed that the most significantly altered and statistically significant category in IbpA-overexpressed