scholarly journals Cytoplasmic Control of Sense-Antisense mRNA Pairs

Cell Reports ◽  
2015 ◽  
Vol 12 (11) ◽  
pp. 1853-1864 ◽  
Author(s):  
Flore Sinturel ◽  
Albertas Navickas ◽  
Maxime Wery ◽  
Marc Descrimes ◽  
Antonin Morillon ◽  
...  
Keyword(s):  
Antisense Mrna

scholarly journals Human retroviral antisense mRNAs are retained in the nuclei of infected cells for viral persistence

2021 ◽  
Vol 118 (17) ◽  
pp. e2014783118
Author(s):  
Guangyong Ma ◽  
Jun-ichirou Yasunaga ◽  
Kazuya Shimura ◽  
Keiko Takemoto ◽  
Miho Watanabe ◽  
...  
Keyword(s):  
Viral Persistence ◽  
Protein Translation ◽  
Regulatory Function ◽  
Antisense Gene ◽  
Cell Leukemia Virus Type ◽  
Antisense Mrna ◽  
Human T Cell ◽  
Infected Cells ◽  
Hiv 1

Human retroviruses, including human T cell leukemia virus type 1 (HTLV-1) and HIV type 1 (HIV-1), encode an antisense gene in the negative strand of the provirus. Besides coding for proteins, the messenger RNAs (mRNAs) of retroviral antisense genes have also been found to regulate transcription directly. Thus, it has been proposed that retroviruses likely localize their antisense mRNAs to the nucleus in order to regulate nuclear events; however, this opposes the coding function of retroviral antisense mRNAs that requires a cytoplasmic localization for protein translation. Here, we provide direct evidence that retroviral antisense mRNAs are localized predominantly in the nuclei of infected cells. The retroviral 3′ LTR induces inefficient polyadenylation and nuclear retention of antisense mRNA. We further reveal that retroviral antisense RNAs retained in the nucleus associate with chromatin and have transcriptional regulatory function. While HTLV-1 antisense mRNA is recruited to the promoter of C-C chemokine receptor type 4 (CCR4) and enhances transcription from it to support the proliferation of HTLV-1–infected cells, HIV-1 antisense mRNA is recruited to the viral LTR and inhibits sense mRNA expression to maintain the latency of HIV-1 infection. In summary, retroviral antisense mRNAs are retained in nucleus, act like long noncoding RNAs instead of mRNAs, and contribute to viral persistence.

Does Vitamin D play a role on Msx1 homeoprotein expression involving an endogenous antisense mRNA?

2004 ◽  
Vol 89-90 ◽  
pp. 413-417 ◽  
Author(s):  
F. Lézot ◽  
A. Coudert ◽  
S. Petit ◽  
B. Vi-Fane ◽  
D. Hotton ◽  
...  
Keyword(s):  
Vitamin D ◽  
Antisense Mrna

scholarly journals A mechanism of suppression of TGF–β/SMAD signaling by NF-κB/RelA

2000 ◽  
Vol 14 (2) ◽  
pp. 187-197 ◽  
Author(s):  
Markus Bitzer ◽  
Gero von Gersdorff ◽  
Dan Liang ◽  
Alfredo Dominguez-Rosales ◽  
Amer A. Beg ◽  
...  
Keyword(s):  
Transforming Growth Factor ◽  
Nuclear Translocation ◽  
Transforming Growth Factor Β ◽  
Nuclear Factor Κb ◽  
Transcriptional Responses ◽  
Smad Signaling ◽  
Antisense Mrna ◽  
Tnf Α ◽  
Factor Α ◽  
Necrosis Factor

A number of pathogenic and proinflammatory stimuli, and the transforming growth factor-β (TGF-β) exert opposing activities in cellular and immune responses. Here we show that the RelA subunit of nuclear factor κB (NF-κB/RelA) is necessary for the inhibition of TGF-β-induced phosphorylation, nuclear translocation, and DNA binding of SMAD signaling complexes by tumor necrosis factor-α (TNF-α). The antagonism is mediated through up-regulation of Smad7 synthesis and induction of stable associations between ligand-activated TGF-β receptors and inhibitory Smad7. Down-regulation of endogenous Smad7 by expression of antisense mRNA releases TGF-β/SMAD-induced transcriptional responses from suppression by cytokine-activated NF-κB/RelA. Following stimulation with bacterial lipopolysaccharide (LPS), or the proinflammatory cytokines TNF-α and interleukin-1β (IL-1β, NF-κB/RelA induces Smad7 synthesis through activation of Smad7 gene transcription. These results suggest a mechanism of suppression of TGF-β/SMAD signaling by opposing stimuli mediated through the activation of inhibitory Smad7 by NF-κB/RelA.

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