The 5′-UTR of DDB2 harbors an IRES element and upregulates translation during stress conditions

Dai, Wenyan; Ma, Wu; Li, Qi; Yifen, Tao; Ding, Pengpeng; Zhu, Ruiyu; Jin, Jian

doi:10.1016/j.gene.2015.07.032

Cited by 10 publications

(7 citation statements)

References 38 publications

(43 reference statements)

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“…The detected 5′ UTR sequences in this study were synthesized by Sangon Biotech Co. (Shanghai, China) and were inserted into bicistronic plasmids between Renilla and firefly luciferase encoding genes. Bicistronic plasmids were constructed based on the pRF vector and has been described previously [ 41 ]. pBRF was constructed by deleting the SV40 promoter from pRF and used to analyze the cryptic promoter.…”

Section: Methodsmentioning

confidence: 99%

La Autoantigen Induces Ribosome Binding Protein 1 (RRBP1) Expression through Internal Ribosome Entry Site (IRES)-Mediated Translation during Cellular Stress Condition

Gao

Zhu

et al. 2016

IJMS

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The function of ribosome binding protein 1 (RRBP1) is regulating the transportation and secretion of some intracellular proteins in mammalian cells. Transcription of RRBP1 is induced by various cytokines. However, few studies focused on the process of RRPB1 mRNA translation. The RRBP1 mRNA has a long 5′ untranslated region that potentially formed a stable secondary structure. In this study, we show that the 5′ UTR of RRBP1 mRNA contains an internal ribosome entry site (IRES). Moreover, the RRBP1 expression is induced by chemotherapeutic drug paclitaxel or adriamycin in human hepatocellular carcinoma cells and accompanied with the increased expression of La autoantigen (La), which binds to RRBP1 IRES element and facilitates translation initiation. Interestingly, we found IRES-mediated RRBP1 translation is also activated during serum-starvation condition which can induce cytoplasmic localization of La. After mapping the entire RRBP1 5′ UTR, we determine the core IRES activity is located between nt-237 and -58. Furthermore, two apical GARR loops within the functional RRBP1 IRES elements may be important for La binding. These results strongly suggest an important role for IRES-dependent translation of RRBP1 mRNA in hepatocellular carcinoma cells during cellular stress conditions.

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Section: Methodsmentioning

confidence: 99%

La Autoantigen Induces Ribosome Binding Protein 1 (RRBP1) Expression through Internal Ribosome Entry Site (IRES)-Mediated Translation during Cellular Stress Condition

Gao

Zhu

et al. 2016

IJMS

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“…Internal ribosome entry sites (IRESs), commonly found in viral RNAs but also present in some eukaryotic transcripts (Weingarten-Gabbay et al 2016), are highly structured regions in the 5 0 UTR that promote translation initiation in a cap-independent fashion (Dai et al 2015). The 5 0 UTR of hepatitis C virus (HCV), which contains a well-characterized IRES (Khawaja et al 2015), is thought to also hijack aspects of the cellular RNAi machinery to stabilize its own RNA and increase translation of viral products.…”

Section: Hepatitis C Virusmentioning

confidence: 99%

The Interplay between the RNA Decay and Translation Machinery in Eukaryotes

Heck

Wilusz

2018

Cold Spring Harb Perspect Biol

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RNA decay plays a major role in regulating gene expression and is tightly networked with other aspects of gene expression to effectively coordinate post-transcriptional regulation. The goal of this work is to provide an overview of the major factors and pathways of general messenger RNA (mRNA) decay in eukaryotic cells, and then discuss the effective interplay of this cytoplasmic process with the protein synthesis machinery. Given the transcript-specific and fluid nature of mRNA stability in response to changing cellular conditions, understanding the fundamental networking between RNA decay and translation will provide a foundation for a complete mechanistic understanding of this important aspect of cell biology.

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“…Renilla luciferase (first cistron, RL) and firefly luciferase (second cistron, FL) was described previously (31,32). To obtain plasmids pR-NRF-F and pR-AHR-F, we inserted the 5'-UTRs of AHR and NRF which were synthesized by Sangon Biotech.…”

Section: Construction Of Dicistronic Reporter Plasmids the Initial Dmentioning

confidence: 99%

Paclitaxel-mediated human aryl hydrocarbon receptor mRNA translation by an internal ribosomal entry site-dependent mechanism

Gao

Sun

et al. 2017

Oncology Reports

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The aryl hydrocarbon receptor (AHR) is a ligand-activated transcription factor that is best known in mediating the toxicities of dioxins and dioxin-like compounds. AHR is activated by a variety of endogenous ligands and participating in tumor development. Thus, it will provide a new approach for cancer prevention and treatment to study the translation mechanism of AHR in tumor cells. In this study, we show that the 5'-untranslated region (UTR) of AHR mRNA contains an internal ribosome entry site (IRES). After mapping the entire AHR 5'-UTR, we determined that the full-length 5'-UTR is indispensable for the highest IRES activity. Interestingly, we found that AHR expression is induced in ovarian (A2780), breast (MDA-MB231), hepatic (Bel7402) and colorectal cancer cells (SW620) by chemotherapeutic drug paclitaxel (PTX) through IRES-dependent translation mechanism. Moreover, IRES activity is increased in the PTX-resistant ovarian cancer cells in which AHR protein expression was also enhanced. These results strongly suggest an important role for AHR IRES-dependent translation mechanism in cancer cell response to paclitaxel treatment.

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The 5′-UTR of DDB2 harbors an IRES element and upregulates translation during stress conditions

Cited by 10 publications

References 38 publications

La Autoantigen Induces Ribosome Binding Protein 1 (RRBP1) Expression through Internal Ribosome Entry Site (IRES)-Mediated Translation during Cellular Stress Condition

La Autoantigen Induces Ribosome Binding Protein 1 (RRBP1) Expression through Internal Ribosome Entry Site (IRES)-Mediated Translation during Cellular Stress Condition

The Interplay between the RNA Decay and Translation Machinery in Eukaryotes

Paclitaxel-mediated human aryl hydrocarbon receptor mRNA translation by an internal ribosomal entry site-dependent mechanism

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