BiP Internal Ribosomal Entry Site Activity Is Controlled by Heat-Induced Interaction of NSAP1

Cho, Sungchan; Park, Sung Mi; Kim, Tae-Don; Kim, Jong Heon; Kim, Kyong‐Tai; Jang, Sung Key

doi:10.1128/mcb.00814-06

Cited by 44 publications

(40 citation statements)

References 44 publications

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“…Activation occurs between 8 and 24 hpi, the same time during infection when increased BiP is first detected. Several cellular proteins have been implicated in the translational activity of the BiP IRES; these include NS1-associated protein 1 (NSAP1), SSB/La autoantigen, p50, and p95 (6,14,31). SSB/La is of particular interest because it is involved in translational activation from IRESs during both poliovirus and hepatitis C virus infections (1,21).…”

Section: Discussionmentioning

confidence: 99%

Human Cytomegalovirus Induces the Endoplasmic Reticulum Chaperone BiP through Increased Transcription and Activation of Translation by Using the BiP Internal Ribosome Entry Site

Buchkovich

Pierciey

et al. 2010

J Virol

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Section: Discussionmentioning

confidence: 99%

Human Cytomegalovirus Induces the Endoplasmic Reticulum Chaperone BiP through Increased Transcription and Activation of Translation by Using the BiP Internal Ribosome Entry Site

Buchkovich

Pierciey

et al. 2010

J Virol

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“…Control or hnRNP Q-specific siRNA-transfected NIH 3T3 cells were treated with cycloheximide (100 g/ml) for 5 min at 37°C and then harvested. Cell extracts were subjected to sucrose gradient analysis, as previously described (9,35). Total RNA of each fraction was purified using TRI reagent (Molecular Research Center) and subjected to real-time PCR analysis for quantification.…”

Section: Methodsmentioning

confidence: 99%

Rhythmic Interaction between Period1 mRNA and hnRNP Q Leads to Circadian Time-Dependent Translation

Lee

Woo

Kim

et al. 2012

Molecular and Cellular Biology

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The mouse PERIOD1 (mPER1) protein, along with other clock proteins, plays a crucial role in the maintenance of circadian rhythms. mPER1 also provides an important link between the circadian system and the cell cycle system. Here we show that the circadian expression of mPER1 is regulated by rhythmic translational control of mPer1 mRNA together with transcriptional modulation. This time-dependent translation was controlled by an internal ribosomal entry site (IRES) element in the 5= untranslated region (5=-UTR) of mPer1 mRNA along with the trans-acting factor mouse heterogeneous nuclear ribonucleoprotein Q (mhnRNP Q). Knockdown of mhnRNP Q caused a decrease in mPER1 levels and a slight delay in mPER1 expression without changing mRNA levels. The rate of IRES-mediated translation exhibits phase-dependent characteristics through rhythmic interactions between mPer1 mRNA and mhnRNP Q. Here, we demonstrate 5=-UTR-mediated rhythmic mPer1 translation and provide evidence for posttranscriptional regulation of the circadian rhythmicity of core clock genes.

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“…Total RNA was extracted using the TRI reagent (Invitrogen). Total RNA (20 g) from transfected 293T cells was analyzed by Northern blot analysis (8). Total RNA (2 g) was reverse transcribed using Improm II reverse transcriptase (Promega), and the cDNA was subjected to real-time PCR analysis for quantification using Sybr premix Ex Taq (Takara).…”

mentioning

confidence: 99%

“…Huh 5-15 cells were subjected to sucrose gradient analysis, as described elsewhere (8). Fractionated samples were classified as shown below in Fig.…”

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confidence: 99%

RNA-Binding Protein hnRNP D Modulates Internal Ribosome Entry Site-Dependent Translation of Hepatitis C Virus RNA

Paek

Kim

Park

et al. 2008

J Virol

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Hepatitis C virus (HCV), one of the major causative agents of virus-related liver cirrhosis and hepatocellular carcinoma in humans, contains a single-stranded RNA genome of positive polarity. HCV RNA contains nontranslated regions (NTRs) at the 5Ј and 3Ј ends (18,23) and a long open reading frame encoding polyprotein that is synthesized through a single translational initiation event directed by an RNA element designated the internal ribosomal entry site (IRES) (21, 38) at the 5Ј NTR (46). The polyprotein is proteolytically processed into 10 or more viral proteins.In general, IRES elements need several canonical translation factors (except eukaryotic initiation factor 4E [eIF4E]) for their activities (40,42). However, HCV IRES-dependent translation requires only a few canonical factors (eIF2, eIF3, eIF5, and eIF5B) for function (30,39,41). Additionally, cellular proteins known as IRES-specific cellular transacting factors (ITAFs) are required for the efficient translation of HCV mRNA. For instance, polypyrimidine tract-binding protein (PTB) interacting with HCV IRES is required for IRES function (2, 3). La antigen interacting with the GCAC site near the initiator AUG is necessary for the optimal function of the HCV IRES (1, 10, 43). Recent studies have shown that NSAP1 interacting with the adenosine-rich core-coding region of HCV mRNA augments HCV IRES-dependent translation (27).Heterogeneous ribonucleoprotein D (hnRNP D), also known as AU-rich element RNA-binding protein 1 (AUF1), is an hnRNP family member that shuttles between the nucleus and cytoplasm (44, 48). hnRNP D was initially identified owing to its ability to bind and destabilize c-myc mRNA in a crude in vitro decay system (6). The protein has four isoforms of different molecular weights (p37, p40, p42, and p45), all of which are produced by alternate splicing of a single transcript (11,47). The hnRNP D protein has various functions, including mRNA decay (6), telomere maintenance (12) MATERIALS AND METHODSPlasmid construction and small interfering RNA (siRNA). Dual reporters harboring the HCV IRES, encephalomyocarditis virus (EMCV) IRES, and cmyc IRES were constructed as described previously (27). The monocistronic reporter containing the HCV IRES and EMCV IRES, followed by firefly luciferase used for in vitro translation, were prepared according to methods described in a previous report (28). Plasmids expressing hnRNP D, pFLAG-CMV2 p37, pFLAG-CMV2 p40, pFLAG-CMV2 p42, and pFLAG-CMV2 p45 were kindly provided by R. J. Schneider at New York University School of Medicine (44). To generate pRSET A-hnRNP D for recombinant hnRNP D purification, pFLAG-CMV2 p45 was treated with HindIII-Klenow-EcoRI, and the resulting DNA fragment was cloned into NcoI-Klenow-EcoRI-treated pRSET A (Invitrogen).To construct pH(130-228)CAT and pH(229-402)CAT used for generating an RNA probe (see Fig. 2B, below), HCV IRES corresponding to positions 130 to 228 and 229 to 402 were amplified from pH(18-402)CAT (27) using the following primer pairs: 5Ј-CTAGGTACCGGGAGAGCCATAG-3Ј and 5...

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BiP Internal Ribosomal Entry Site Activity Is Controlled by Heat-Induced Interaction of NSAP1

Cited by 44 publications

References 44 publications

Human Cytomegalovirus Induces the Endoplasmic Reticulum Chaperone BiP through Increased Transcription and Activation of Translation by Using the BiP Internal Ribosome Entry Site

Human Cytomegalovirus Induces the Endoplasmic Reticulum Chaperone BiP through Increased Transcription and Activation of Translation by Using the BiP Internal Ribosome Entry Site

Rhythmic Interaction between Period1 mRNA and hnRNP Q Leads to Circadian Time-Dependent Translation

RNA-Binding Protein hnRNP D Modulates Internal Ribosome Entry Site-Dependent Translation of Hepatitis C Virus RNA

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