scholarly journals Substrate Recognition and Specificity of Double-Stranded RNA Binding Proteins

Biochemistry ◽  
2014 ◽  
Vol 53 (21) ◽  
pp. 3457-3466 ◽  
Author(s):  
Lela Vuković ◽  
Hye Ran Koh ◽  
Sua Myong ◽  
Klaus Schulten
Keyword(s):  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Substrate Recognition ◽  
Double Stranded Rna

scholarly journals Substrate Recognition and Specificity of Double-Stranded RNA Binding Proteins

2014 ◽  
Vol 106 (2) ◽  
pp. 22a
Author(s):  
Lela Vukovic ◽  
Hye Ran Koh ◽  
Sua Myong ◽  
Klaus Schulten
Keyword(s):  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Substrate Recognition ◽  
Double Stranded Rna

Characterization of Viral Double-Stranded RNA-Binding Proteins

Methods ◽  
1998 ◽  
Vol 15 (3) ◽  
pp. 225-232 ◽  
Author(s):  
Bertram L. Jacobs ◽  
Jeffrey O. Langland ◽  
Teresa Brandt
Keyword(s):  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Double Stranded Rna

Double-stranded RNA-binding Proteins and the Control of Protein Synthesis and Cell Growth

2001 ◽  
Vol 66 (0) ◽  
pp. 485-498 ◽  
Author(s):  
L.M. PARKER ◽  
I. FIERRO-MONTI ◽  
T.W. REICHMAN ◽  
S. GUNNERY ◽  
M.B. MATHEWS
Keyword(s):  
Protein Synthesis ◽  
Cell Growth ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Double Stranded Rna

scholarly journals Know Thyself: RIG-I-Like Receptor Sensing of DNA Virus Infection

2019 ◽  
Vol 93 (23) ◽  
Author(s):  
Yang Zhao ◽  
John Karijolich
Keyword(s):  
Virus Infection ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Rna Virus ◽  
Intrinsic Immunity ◽  
Dna Virus ◽  
Double Stranded Rna ◽  
Recent Advances

ABSTRACT The RIG-I-like receptors (RLRs) are double-stranded RNA-binding proteins that play a role in initiating and modulating cell intrinsic immunity through the recognition of RNA features typically absent from the host transcriptome. While they are initially characterized in the context of RNA virus infection, evidence has now accumulated establishing the role of RLRs in DNA virus infection. Here, we review recent advances in the RLR-mediated restriction of DNA virus infection with an emphasis on the RLR ligands sensed.

scholarly journals Dynamic profiling of double-stranded RNA binding proteins

2015 ◽  
Vol 43 (15) ◽  
pp. 7566-7576 ◽  
Author(s):  
Xinlei Wang ◽  
Lela Vukovic ◽  
Hye Ran Koh ◽  
Klaus Schulten ◽  
Sua Myong
Keyword(s):  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Double Stranded Rna ◽  
Dynamic Profiling

Selective Regulation of Gene Expression by Nuclear Factor 110, a Member of the NF90 Family of Double-stranded RNA-binding Proteins

2003 ◽  
Vol 332 (1) ◽  
pp. 85-98 ◽  
Author(s):  
Trevor W. Reichman ◽  
Andrew M. Parrott ◽  
Ivo Fierro-Monti ◽  
David J. Caron ◽  
Peter N. Kao ◽  
...  
Keyword(s):  
Gene Expression ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Regulation Of Gene Expression ◽  
Nuclear Factor ◽  
Double Stranded Rna

scholarly journals Double-stranded RNA binding proteins DRB2 and DRB4 have an antagonistic impact on polymerase IV-dependent siRNA levels in Arabidopsis

RNA ◽  
2011 ◽  
Vol 17 (8) ◽  
pp. 1502-1510 ◽  
Author(s):  
T. Pelissier ◽  
M. Clavel ◽  
C. Chaparro ◽  
M.-N. Pouch-Pelissier ◽  
H. Vaucheret ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Double Stranded Rna

scholarly journals Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins

2002 ◽  
Vol 156 (1) ◽  
pp. 53-64 ◽  
Author(s):  
Amy M. Brownawell ◽  
Ian G. Macara
Keyword(s):  
Nuclear Export ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Dependent Manner ◽  
Intact Cells ◽  
Double Stranded Rna ◽  
Permeabilized Cells ◽  
Dsrna Binding ◽  
Rna Export

We have identified a novel human karyopherin (Kap)β family member that is related to human Crm1 and the Saccharomyces cerevisiae protein, Msn5p/Kap142p. Like other known transport receptors, this Kap binds specifically to RanGTP, interacts with nucleoporins, and shuttles between the nuclear and cytoplasmic compartments. We report that interleukin enhancer binding factor (ILF)3, a double-stranded RNA binding protein, associates with this Kap in a RanGTP-dependent manner and that its double-stranded RNA binding domain (dsRBD) is the limiting sequence required for this interaction. Importantly, the Kap interacts with dsRBDs found in several other proteins and binding is blocked by double-stranded RNA. We find that the dsRBD of ILF3 functions as a novel nuclear export sequence (NES) in intact cells, and its ability to serve as an NES is dependent on the expression of the Kap. In digitonin-permeabilized cells, the Kap but not Crm1 stimulated nuclear export of ILF3. Based on the ability of this Kap to mediate the export of dsRNA binding proteins, we named the protein exportin-5. We propose that exportin-5 is not an RNA export factor but instead participates in the regulated translocation of dsRBD proteins to the cytoplasm where they interact with target mRNAs.

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