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Transformation of eEF1Bδ into heat-shock response transcription factor by alternative splicing.

ABSTRACT: Protein translation factors have crucial roles in a variety of stress responses. Here, we show that eukaryotic elongation factor 1Bδ (eEF1Bδ) changes its structure and function from a translation factor into a heat-shock response transcription factor by alternative splicing. The long isoform of eEF1Bδ (eEF1BδL) is localized in the nucleus and induces heat-shock element (HSE)-containing genes in cooperation with heat-shock transcription factor 1 (HSF1). Moreover, the amino-terminal domain of eEF1BδL binds to NF-E2-related factor 2 (Nrf2) and induces stress response haem oxygenase 1 (HO1). Specific inhibition of eEF1BδL with small-interfering RNA completely inhibits Nrf2-dependent HO1 induction. In addition, eEF1BδL directly binds to HSE oligo DNA in vitro and associates with the HSE consensus in the HO1 promoter region in vivo. Thus, the transcriptional role of eEF1BδL could provide new insights into the molecular mechanism of stress responses.

SUBMITTER: Kaitsuka T

PROVIDER: S-EPMC3128969 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature

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Transformation of eEF1Bδ into heat-shock response transcription factor by alternative splicing.

Kaitsuka Taku T Tomizawa Kazuhito K Matsushita Masayuki M

EMBO reports 20110701 7

Protein translation factors have crucial roles in a variety of stress responses. Here, we show that eukaryotic elongation factor 1Bδ (eEF1Bδ) changes its structure and function from a translation factor into a heat-shock response transcription factor by alternative splicing. The long isoform of eEF1Bδ (eEF1BδL) is localized in the nucleus and induces heat-shock element (HSE)-containing genes in cooperation with heat-shock transcription factor 1 (HSF1). Moreover, the amino-terminal domain of eEF1 ...[more]

PMID: 21597468

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Project description:White-rot fungi, especially Trametes strains, are the primary source of industrial laccases in bioenergy and bioremediation. Trametes strains express members of the laccase gene family with different physicochemical properties and expression patterns. However, the literature on the expression pattern of the laccase gene family in T. trogii S0301 and the response mechanism to Cu2+, a key laccase inducer, in white-rot fungal strains is scarce. In the present study, we found that Cu2+ could induce the mRNAs and proteins of the two alternative splicing variants of heat shock transcription factor 2 (TtHSF2). Furthermore, the overexpression of alternative splicing variants TtHSF2α and TtHSF2β-I in the homokaryotic T. trogii S0301 strain showed opposite effects on the extracellular total laccase activity, with the maximum laccase activity of approximately 0.6 U mL-1 and 3.0 U mL-1, respectively, on the eighth day, which is 0.4 and 2.3 times that of the wild type strain. Similarly, TtHSF2α and TtHSF2β-I play opposite roles in the oxidation tolerance to H2O2 In addition, the direct binding of TtHSF2α to the promoter regions of the representative laccase isoenzymes (TtLac1 and TtLac13) and protein-protein interactions between TtHSF2α and TtHSF2β-I were detected. Our results demonstrate the crucial roles of TtHSF2 and its alternative splicing variants in response to Cu2+ We believe that these findings will deepen our understanding of alternative splicing of HSFs and their regulatory mechanism of the laccase gene family in white-rot fungi.Importance The members of laccase gene family in Trametes strains are the primary source of industrial laccase and have gained widespread attention. Increasing the yield and enzymatic properties of laccase through various methods has always been a topic worthy of attention, and there is no report on the regulation of laccase expression through HSF transcription factor engineering. Here, we found that two alternative splicing variants of TtHSF2 functioned oppositely in regulating the expression of laccase genes, and copper can induce the expression of almost all members of the laccase gene family. Most importantly, our study suggested that TtHSF2 and its alternative splicing variants are vital for copper-induced production of laccases in T. trogii S0301.

Dataset Information

Transformation of eEF1Bδ into heat-shock response transcription factor by alternative splicing.

Publications

Transformation of eEF1Bδ into heat-shock response transcription factor by alternative splicing.

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