Transformation of eEF1Bdelta into heat-shock response transcription factor by alternative splicing.

Article Details

Citation

Kaitsuka T, Tomizawa K, Matsushita M

Transformation of eEF1Bdelta into heat-shock response transcription factor by alternative splicing.

EMBO Rep. 2011 Jul 1;12(7):673-81. doi: 10.1038/embor.2011.82.

PubMed ID
21597468 [ View in PubMed
]
Abstract

Protein translation factors have crucial roles in a variety of stress responses. Here, we show that eukaryotic elongation factor 1Bdelta (eEF1Bdelta) changes its structure and function from a translation factor into a heat-shock response transcription factor by alternative splicing. The long isoform of eEF1Bdelta (eEF1BdeltaL) 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 eEF1BdeltaL binds to NF-E2-related factor 2 (Nrf2) and induces stress response haem oxygenase 1 (HO1). Specific inhibition of eEF1BdeltaL with small-interfering RNA completely inhibits Nrf2-dependent HO1 induction. In addition, eEF1BdeltaL 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 eEF1BdeltaL could provide new insights into the molecular mechanism of stress responses.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Heat shock factor protein 1Q00613Details
Nuclear factor erythroid 2-related factor 2Q16236Details