RNA Helicase p68 Deploys β-Catenin in Regulating RelA/P65 Gene Expression

2019 ◽  
Author(s):  
Veenita Khare ◽  
Shaheda Tabassum ◽  
Uttara Chatterjee ◽  
Sandip Chatterjee ◽  
Mrinal K. Ghosh
Keyword(s):  
Gene Expression ◽  
Rna Helicase ◽  
Rna Helicase P68

scholarly journals RNA helicase p68 deploys β-catenin in regulating RelA/p65 gene expression: implications in colon cancer

2019 ◽  
Vol 38 (1) ◽  
Author(s):  
Veenita Khare ◽  
Shaheda Tabassum ◽  
Uttara Chatterjee ◽  
Sandip Chatterjee ◽  
Mrinal K. Ghosh
Keyword(s):  
Gene Expression ◽  
Colon Cancer ◽  
Rna Helicase ◽  
Rna Helicase P68

scholarly journals Cellular RNA Helicase p68 Relocalization and Interaction with the Hepatitis C Virus (HCV) NS5B Protein and the Potential Role of p68 in HCV RNA Replication

2004 ◽  
Vol 78 (10) ◽  
pp. 5288-5298 ◽  
Author(s):  
Phuay-Yee Goh ◽  
Yee-Joo Tan ◽  
Siew Pheng Lim ◽  
Y. H. Tan ◽  
Seng Gee Lim ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Cell Line ◽  
Rna Helicase ◽  
Hcv Rna ◽  
Activity Levels ◽  
Nonstructural Proteins ◽  
Negative Strand ◽  
Replicon Cell Line ◽  
Rna Helicase P68

ABSTRACT Chronic infection by hepatitis C virus (HCV) can lead to severe hepatitis and cirrhosis and is closely associated with hepatocellular carcinoma. The replication cycle of HCV is poorly understood but is likely to involve interaction with host factors. In this report, we show that NS5B, the HCV RNA-dependent RNA polymerase (RdRp), interacts with a human RNA helicase, p68. Transient expression of NS5B alone, as well as the stable expression of all the nonstructural proteins in a HCV replicon-bearing cell line (V. Lohmann, F. Korner, J.-O. Koch, U. Herian, L. Theilmann, and R. Bartenschlager, Science 285:110-113), causes the redistribution of endogenous p68 from the nucleus to the cytoplasm. Deletion of the C-terminal two-thirds of NS5B (NS5BΔC) dramatically reduces its coimmunoprecipitation (co-IP) with endogenous p68, while the deletion of the N-terminal region (NS5BΔN1 and NS5BΔN2) does not affect its interaction with p68. In consistency with the co-IP results, NS5BΔC does not cause the relocalization of p68 whereas NS5BΔN1 does. With a replicon cell line, we were not able to detect a change in positive- and negative-strand synthesis when p68 levels were reduced using small interfering RNA (siRNA). In cells transiently transfected with a full-length HCV construct, however, the depletion (using specific p68 siRNA) of endogenous p68 correlated with a reduction in the transcription of negative-strand from positive-strand HCV RNA. Overexpression of NS5B and NS5BΔN1, but not that of NS5BΔC, causes a reduction in the negative-strand synthesis, indicating that overexpressed NS5B and NS5BΔN1 sequesters p68 from the replication complexes (thus reducing their replication activity levels). Identification of p68 as a cellular factor involved in HCV replication, at least for cells transiently transfected with a HCV expression construct, is a step towards understanding HCV replication.

scholarly journals The RNA helicase DDX5 promotes alveolar rhabdomyosarcoma growth and survival

2020 ◽  
Author(s):  
Alberto Gualtieri ◽  
Valerio Licursi ◽  
Chiara Mozzetta
Keyword(s):  
Gene Expression ◽  
Soft Tissue ◽  
Soft Tissue Sarcoma ◽  
Therapeutic Target ◽  
Rna Helicase ◽  
Potential Therapeutic Target ◽  
Growth And Survival ◽  
Dead Box ◽  
Pharmacological Targets ◽  
Xenograft Models

AbstractRhabdomyosarcoma (RMS) is the most common soft-tissue sarcoma of childhood characterized by the inability to exit the proliferative myoblast-like stage. The alveolar fusion positive subtype (FP-ARMS) is the most aggressive and is mainly caused by the expression of PAX3/7-FOXO1 oncoproteins, which are challenging pharmacological targets. Thus, other therapeutic vulnerabilities resulting from gene expression changes are progressively being recognized. Here, we identified the DEAD box RNA helicase 5 (DDX5) as a potential therapeutic target to inhibit FP-ARMS growth. We show that DDX5 is overexpressed in alveolar RMS cells, demonstrating that its depletion drastically decreases FP-ARMS viability and slows tumor growth in xenograft models. Mechanistically, we provide evidence that DDX5 functions upstream the G9a/AKT survival signalling pathway, by modulating G9a protein stability. Finally, we show that G9a interacts with PAX3-FOXO1 and regulates its activity, thus sustaining FP-ARMS myoblastic state. Together, our findings identify a novel survival-promoting loop in FP-ARMS and highlight DDX5 as potential therapeutic target to arrest rhabdomyosarcoma growth.

scholarly journals The RNA helicase p68 (DDX5) is selectively required for the induction of p53-dependent p21 expression and cell-cycle arrest after DNA damage

Oncogene ◽  
2012 ◽  
Vol 32 (29) ◽  
pp. 3461-3469 ◽  
Author(s):  
S M Nicol ◽  
S E Bray ◽  
H Derek Black ◽  
S A Lorimore ◽  
E G Wright ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Dna Damage ◽  
Cell Cycle Arrest ◽  
Rna Helicase ◽  
Cycle Arrest ◽  
Rna Helicase P68

scholarly journals The ATP-Dependent RNA Helicase DDX3X Modulates Herpes Simplex Virus 1 Gene Expression

2017 ◽  
Vol 91 (8) ◽  
Author(s):  
Bita Khadivjam ◽  
Camille Stegen ◽  
Marc-Aurèle Hogue-Racine ◽  
Nabil El Bilali ◽  
Katinka Döhner ◽  
...  
Keyword(s):  
Gene Expression ◽  
Herpes Simplex ◽  
Rna Viruses ◽  
Rna Helicase ◽  
Viral Gene ◽  
Herpes Simplex Virus 1 ◽  
Dna Viruses ◽  
Viral Particles ◽  
Simplex Virus ◽  
Hsv 1

ABSTRACT The human protein DDX3X is a DEAD box ATP-dependent RNA helicase that regulates transcription, mRNA maturation, and mRNA export and translation. DDX3X concomitantly modulates the replication of several RNA viruses and promotes innate immunity. We previously showed that herpes simplex virus 1 (HSV-1), a human DNA virus, incorporates DDX3X into its mature particles and that DDX3X is required for optimal HSV-1 infectivity. Here, we show that viral gene expression, replication, and propagation depend on optimal DDX3X protein levels. Surprisingly, DDX3X from incoming viral particles was not required for the early stages of the HSV-1 infection, but, rather, the protein controlled the assembly of new viral particles. This was independent of the previously reported ability of DDX3X to stimulate interferon type I production. Instead, both the lack and overexpression of DDX3X disturbed viral gene transcription and thus subsequent genome replication. This suggests that in addition to its effect on RNA viruses, DDX3X impacts DNA viruses such as HSV-1 by an interferon-independent pathway. IMPORTANCE Viruses interact with a variety of cellular proteins to complete their life cycle. Among them is DDX3X, an RNA helicase that participates in most aspects of RNA biology, including transcription, splicing, nuclear export, and translation. Several RNA viruses and a limited number of DNA viruses are known to manipulate DDX3X for their own benefit. In contrast, DDX3X is also known to promote interferon production to limit viral propagation. Here, we show that DDX3X, which we previously identified in mature HSV-1 virions, stimulates HSV-1 gene expression and, consequently, virion assembly by a process that is independent of its ability to promote the interferon pathway.

scholarly journals Substrate Specificity of the TRAMP Nuclear Surveillance Complexes

2020 ◽  
Author(s):  
Clémentine Delan-Forino ◽  
Christos Spanos ◽  
Juri Rappsilber ◽  
David Tollervey
Keyword(s):  
Gene Expression ◽  
Mass Spectrometry ◽  
Binding Sites ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Rna Binding Protein ◽  
Rna Helicase ◽  
Nuclear Rna ◽  
Rna Exosome

ABSTRACTDuring nuclear surveillance in yeast, the RNA exosome functions together with the TRAMP complexes. These include the DEAH-box RNA helicase Mtr4 together with an RNA-binding protein (Air1 or Air2) and a poly(A) polymerase (Trf4 or Trf5). To better determine how RNA substrates are targeted, we analyzed protein and RNA interactions for TRAMP components. Mass spectrometry identified three distinct TRAMP complexes formed in vivo. These complexes preferentially assemble on different classes of transcripts. Unexpectedly, on many substrates, including pre-rRNAs and pre-mRNAs, binding specificity was apparently conferred by Trf4 and Trf5. Clustering of mRNAs by TRAMP association showed co-enrichment for mRNAs with functionally related products, supporting the significance of surveillance in regulating gene expression. We compared binding sites of TRAMP components with multiple nuclear RNA binding proteins, revealing preferential colocalization of subsets of factors. TRF5 deletion reduced Mtr4 recruitment and increased RNA abundance for mRNAs specifically showing high Trf5 binding.

scholarly journals RNA Helicase p68 (DDX5) Regulates tau Exon 10 Splicing by Modulating a Stem-Loop Structure at the 5' Splice Site

2011 ◽  
Vol 31 (9) ◽  
pp. 1812-1821 ◽  
Author(s):  
A. Kar ◽  
K. Fushimi ◽  
X. Zhou ◽  
P. Ray ◽  
C. Shi ◽  
...  
Keyword(s):  
Splice Site ◽  
Rna Helicase ◽  
Loop Structure ◽  
Stem Loop ◽  
Stem Loop Structure ◽  
Rna Helicase P68 ◽  
Exon 10

Current view on the helicase activity of RNA helicase A and its role in gene expression

2020 ◽  
Vol 21 ◽  
Author(s):  
Yuan-Qing Pan ◽  
Li Xing
Keyword(s):  
Gene Expression ◽  
Rna Splicing ◽  
Rna Helicase ◽  
Circular Rna ◽  
Nucleoside Triphosphate ◽  
Current View ◽  
Helicase Activity ◽  
Rna Helicase A ◽  
Cellular Processes

: RNA helicase A (RHA) is a DExH-box helicase that plays regulatory roles in a variety of cellular processes including transcription, translation, RNA splicing, editing, transport, and processing, microRNA genesis and maintenance of genomic stability. It is involved in virus replication, oncogenesis, and innate immune response. RHA can unwind nucleic acid duplex by nucleoside triphosphate hydrolysis. The insight into molecular mechanism of helicase activity is fundamental to understanding the role of RHA in the cell. Herein, we reviewed the current advances on the helicase activity of RHA and its relevance to gene expression, particularly, to genesis of circular RNA.

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