scholarly journals Insights into the Structure of Dimeric RNA Helicase CsdA and Indispensable Role of Its C-Terminal Regions

Structure ◽  
2017 ◽  
Vol 25 (12) ◽  
pp. 1795-1808.e5 ◽  
Author(s):  
Ling Xu ◽  
Lijun Wang ◽  
Junhui Peng ◽  
Fudong Li ◽  
Lijie Wu ◽  
...  
Keyword(s):  
Rna Helicase

scholarly journals RNA Helicase A Regulates the Replication of RNA Viruses

Viruses ◽  
2021 ◽  
Vol 13 (3) ◽  
pp. 361
Author(s):  
Rui-Zhu Shi ◽  
Yuan-Qing Pan ◽  
Li Xing
Keyword(s):  
Virus Replication ◽  
Rna Binding ◽  
Rna Viruses ◽  
Rna Helicase ◽  
Rna Helicase A ◽  
Double Stranded Rna ◽  
Binding Domains ◽  
N Terminus

The RNA helicase A (RHA) is a member of DExH-box helicases and characterized by two double-stranded RNA binding domains at the N-terminus. RHA unwinds double-stranded RNA in vitro and is involved in RNA metabolisms in the cell. RHA is also hijacked by a variety of RNA viruses to facilitate virus replication. Herein, this review will provide an overview of the role of RHA in the replication of RNA viruses.

scholarly journals Role of the amino terminal RHAU-specific motif in the recognition and resolution of guanine quadruplex-RNA by the DEAH-box RNA helicase RHAU

2010 ◽  
Vol 38 (18) ◽  
pp. 6219-6233 ◽  
Author(s):  
Simon Lattmann ◽  
Banabihari Giri ◽  
James P. Vaughn ◽  
Steven A. Akman ◽  
Yoshikuni Nagamine
Keyword(s):  
Rna Helicase ◽  
Amino Terminal ◽  
Guanine Quadruplex

scholarly journals A Method to Study the Role of DDX3 RNA Helicase in HIV-1

2009 ◽  
pp. 281-289 ◽  
Author(s):  
Chia-Yen Chen ◽  
Venkat R.K. Yedavalli ◽  
Kuan-Teh Jeang
Keyword(s):  
Rna Helicase ◽  
Hiv 1

The role of the DEAD-box RNA helicase DDX3 in mRNA metabolism

2013 ◽  
Vol 4 (4) ◽  
pp. 369-385 ◽  
Author(s):  
Ricardo Soto-Rifo ◽  
Théophile Ohlmann
Keyword(s):  
Rna Helicase ◽  
Mrna Metabolism ◽  
Dead Box ◽  
The Dead

Viruses and the human DEAD-box helicase DDX3: inhibition or exploitation?

2011 ◽  
Vol 39 (2) ◽  
pp. 679-683 ◽  
Author(s):  
Martina Schröder
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Global Health ◽  
Antiviral Immunity ◽  
Rna Helicase ◽  
Dead Box ◽  
Health Threats ◽  
Prime Target

Human DDX3 is a DEAD (Asp-Glu-Ala-Asp)-box RNA helicase that appears to be a prime target for viral manipulation. While two viruses that manifest major global health threats, HIV and HCV (hepatitis C virus), utilize DDX3 for their replication, other viruses inhibit DDX3's newly identified function in innate antiviral signalling. This review discusses the role of DDX3 in antiviral immunity and its inhibition or exploitation by different viruses.

scholarly journals A DNA-sensing–independent role of a nuclear RNA helicase, DHX9, in stimulation of NF-κB–mediated innate immunity against DNA virus infection

2018 ◽  
Vol 46 (17) ◽  
pp. 9011-9026 ◽  
Author(s):  
Yee Ching Ng ◽  
Woo-Chang Chung ◽  
Hye-Ri Kang ◽  
Hye-Jeong Cho ◽  
Eun-Byeol Park ◽  
...  
Keyword(s):  
Innate Immunity ◽  
Virus Infection ◽  
Rna Helicase ◽  
Dna Sensing ◽  
Dna Virus ◽  
Nuclear Rna ◽  
Stimulation Of

scholarly journals Evaluation of an ASFV RNA Helicase Gene A859L for Virus Replication and Swine Virulence

Viruses ◽  
2021 ◽  
Vol 14 (1) ◽  
pp. 10
Author(s):  
Elizabeth Ramirez-Medina ◽  
Elizabeth A. Vuono ◽  
Sarah Pruitt ◽  
Ayushi Rai ◽  
Nallely Espinoza ◽  
...  
Keyword(s):  
Virus Replication ◽  
Recombinant Virus ◽  
Bioinformatics Analysis ◽  
African Swine Fever Virus ◽  
Geographical Area ◽  
African Swine Fever ◽  
Rna Helicase ◽  
Helicase Gene ◽  
Highly Virulent

African swine fever virus (ASFV) is producing a devastating pandemic that, since 2007, has spread to a contiguous geographical area from central Europe to Asia. In July 2021, ASFV was detected in the Dominican Republic, the first report of the disease in the Americas in more than 40 years. ASFV is a large, highly complex virus harboring a large dsDNA genome that encodes for more than 150 genes. The majority of these genes have not been functionally characterized. Bioinformatics analysis predicts that ASFV gene A859L encodes for an RNA helicase, although its function has not yet been experimentally assessed. Here, we evaluated the role of the A859L gene during virus replication in cell cultures and during infection in swine. For that purpose, a recombinant virus (ASFV-G-∆A859L) harboring a deletion of the A859L gene was developed using the highly virulent ASFV Georgia (ASFV-G) isolate as a template. Recombinant ASFV-G-∆A859L replicates in swine macrophage cultures as efficiently as the parental virus ASFV-G, demonstrating that the A859L gene is non-essential for ASFV replication. Experimental infection of domestic pigs demonstrated that ASFV-G-∆A859L replicates as efficiently and induces a clinical disease indistinguishable from that caused by the parental ASFV-G. These studies conclude that the predicted RNA helicase gene A859L is not involved in the processes of virus replication or disease production in swine.

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.

scholarly journals N6-methyladenosine modification of HCV RNA genome regulates cap-independent IRES-mediated translation via YTHDC2 recognition

2021 ◽  
Vol 118 (10) ◽  
pp. e2022024118 ◽  
Author(s):  
Geon-Woo Kim ◽  
Aleem Siddiqui
Keyword(s):  
Translation Initiation ◽  
Mutational Analysis ◽  
Rna Helicase ◽  
Hcv Rna ◽  
Helicase Domain ◽  
Entry Site ◽  
Ires Element ◽  
Rna Genome ◽  
Hcv Ires

Hepatitis C virus (HCV) infections are associated with the risk of progression to fibrosis, cirrhosis, and hepatocellular carcinoma. The HCV RNA genome is translated by an internal ribosome entry site (IRES)-dependent mechanism. The structure and function of the HCV IRES have been investigated by both biological and biophysical criteria. Recently, the role of N6-methyladenosine (m6A) in cellular RNA and viral transcripts has been intensely investigated. The HCV RNA genome is m6A-methylated, and this modification regulates the viral life cycle. In this study, we investigated the role of m6A modification of the HCV genome in the IRES-dependent translation function by mutating m6A consensus motifs (DRACH) within the IRES element in stem–loop III and IV regions and studied their effect on translation initiation. There are several DRACH motifs within the IRES element. Of these, the DRACH motif at nucleotide (nt) 329-333, located about 7 nt upstream of initiator AUG (iAUG) codon, regulates IRES-mediated translation initiation. Mutational analysis showed that m6A methylation of the adenosine at nt 331 is essential for the IRES-dependent translation. m6A reader protein YTHDC2, containing the RNA helicase domain, recognizes m6A-methylated adenosine at nt 331 and, in concert with the cellular La antigen, supports HCV IRES-dependent translation. The RNA helicase dead YTHDC2 (E332Q) mutant failed to stimulate HCV translation initiation. This report highlights the functional roles of m6A modification and YTHDC2 in the HCV IRES-dependent translation initiation, thus offering alternative therapeutic avenues to interfere with the infectious process.

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