scholarly journals Comparative Mutational Analysis of the Double-stranded RNA Binding Domains ofXenopus laevisRNA-binding Protein A

1996 ◽  
Vol 271 (45) ◽  
pp. 28112-28119 ◽  
Author(s):  
Barbara C. Krovat ◽  
Michael F. Jantsch
Keyword(s):  
Rna Binding ◽  
Mutational Analysis ◽  
Binding Protein ◽  
Protein A ◽  
Double Stranded Rna ◽  
Binding Domains ◽  
Rna Binding Domains

scholarly journals Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein

2010 ◽  
Vol 20 (1) ◽  
pp. 118-130 ◽  
Author(s):  
Seisuke Yamashita ◽  
Takashi Nagata ◽  
Masahito Kawazoe ◽  
Chie Takemoto ◽  
Takanori Kigawa ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Double Stranded Rna ◽  
Binding Domains ◽  
Tar Rna ◽  
Rna Binding Domains

scholarly journals The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities.

1991 ◽  
Vol 11 (7) ◽  
pp. 3419-3424 ◽  
Author(s):  
C G Burd ◽  
E L Matunis ◽  
G Dreyfuss
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Consensus Sequence ◽  
Binding Activity ◽  
Yeast Cells ◽  
Yeast Saccharomyces Cerevisiae ◽  
Amino Terminal ◽  
Binding Domains ◽  
Rna Binding Domains

The poly(A)-binding protein (PABP) is the major mRNA-binding protein in eukaryotes, and it is essential for viability of the yeast Saccharomyces cerevisiae. The amino acid sequence of the protein indicates that it consists of four ribonucleoprotein consensus sequence-containing RNA-binding domains (RBDs I, II, III, and IV) and a proline-rich auxiliary domain at the carboxyl terminus. We produced different parts of the S. cerevisiae PABP and studied their binding to poly(A) and other ribohomopolymers in vitro. We found that none of the individual RBDs of the protein bind poly(A) specifically or efficiently. Contiguous two-domain combinations were required for efficient RNA binding, and each pairwise combination (I/II, II/III, and III/IV) had a distinct RNA-binding activity. Specific poly(A)-binding activity was found only in the two amino-terminal RBDs (I/II) which, interestingly, are dispensable for viability of yeast cells, whereas the activity that is sufficient to rescue lethality of a PABP-deleted strain is in the carboxyl-terminal RBDs (III/IV). We conclude that the PABP is a multifunctional RNA-binding protein that has at least two distinct and separable activities: RBDs I/II, which most likely function in binding the PABP to mRNA through the poly(A) tail, and RBDs III/IV, which may function through binding either to a different part of the same mRNA molecule or to other RNA(s).

scholarly journals Recognition of viral RNA stem-loops by the tandem double-stranded RNA binding domains of PKR

RNA ◽  
2013 ◽  
Vol 19 (3) ◽  
pp. 333-344 ◽  
Author(s):  
E. Dzananovic ◽  
T. R. Patel ◽  
S. Deo ◽  
K. McEleney ◽  
J. Stetefeld ◽  
...  
Keyword(s):  
Rna Binding ◽  
Viral Rna ◽  
Double Stranded Rna ◽  
Binding Domains ◽  
Rna Binding Domains

scholarly journals The N-Terminal Double-Stranded RNA Binding Domains of Arabidopsis HYPONASTIC LEAVES1 Are Sufficient for Pre-MicroRNA Processing

2007 ◽  
Vol 19 (3) ◽  
pp. 914-925 ◽  
Author(s):  
Feijie Wu ◽  
Lin Yu ◽  
Wenguang Cao ◽  
Yanfei Mao ◽  
Zhongyuan Liu ◽  
...  
Keyword(s):  
Rna Binding ◽  
Double Stranded Rna ◽  
Binding Domains ◽  
Microrna Processing ◽  
Rna Binding Domains

Solution structures of the double-stranded RNA-binding domains from rna helicase A

2012 ◽  
Vol 80 (6) ◽  
pp. 1699-1706 ◽  
Author(s):  
Takashi Nagata ◽  
Kengo Tsuda ◽  
Naohiro Kobayashi ◽  
Mikako Shirouzu ◽  
Takanori Kigawa ◽  
...  
Keyword(s):  
Rna Binding ◽  
Rna Helicase ◽  
Rna Helicase A ◽  
Double Stranded Rna ◽  
Solution Structures ◽  
Binding Domains ◽  
Rna Binding Domains

scholarly journals Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless

2018 ◽  
Author(s):  
Pravin Kumar Ankush Jagtap ◽  
Marisa Müller ◽  
Pawel Masiewicz ◽  
Sören von Bülow ◽  
Nele Merret Hollmann ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Motifs ◽  
Double Stranded Rna ◽  
Binding Domains ◽  
Dsrna Binding ◽  
Rna Binding Domains ◽  
Human Orthologue ◽  
Rox Rna

ABSTRACTMaleless (MLE) is an evolutionary conserved member of the DExH family of helicases in Drosophila. Besides its function in RNA editing and presumably siRNA processing, MLE is best known for its role in remodelling non-coding roX RNA in the context of X chromosome dosage compensation in male flies. MLE and its human orthologue, DHX9 contain two tandem double-stranded RNA binding domains (dsRBDs) located at the N-terminal region. The two dsRBDs are essential for localization of MLE at the X-territory and it is presumed that this involves binding roX secondary structures. However, for dsRBD1 roX RNA binding has so far not been described. Here, we determined the solution NMR structure of dsRBD1 and dsRBD2 of MLE in tandem and investigated its role in double-stranded RNA (dsRNA) binding. Our NMR data show that both dsRBDs act as independent structural modules in solution and are canonical, non-sequence-specific dsRBDs featuring non-canonical KKxAK RNA binding motifs. NMR titrations combined with filter binding experiments document the contribution of dsRBD1 to dsRNA binding in vitro. Curiously, dsRBD1 mutants in which dsRNA binding in vitro is strongly compromised do not affect roX2 RNA binding and MLE localization in cells. These data suggest alternative functions for dsRBD1 in vivo.

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