Structural Characterization of RNA Recognition Motif-2 Domain of SART3

2017 ◽  
Vol 38 (4) ◽  
pp. 444-447
Author(s):  
Kyeong-Mi Bang ◽  
Na Youn Cho ◽  
Won-Je Kim ◽  
Ae-Ryung Kim ◽  
Hyun Kyu Song ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Recognition Motif

scholarly journals Functional Dissection of the Human TNRC6 (GW182-Related) Family of Proteins

2009 ◽  
Vol 29 (15) ◽  
pp. 4144-4155 ◽  
Author(s):  
David Baillat ◽  
Ramin Shiekhattar
Keyword(s):  
Mammalian Cells ◽  
Trinucleotide Repeat ◽  
Critical Role ◽  
Functional Characterization ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Critical Function ◽  
Recognition Motif ◽  
Related Family

ABSTRACT Argonaute (Ago) proteins through their association with small RNAs perform a critical function in the effector step of RNA interference. The TNRC6 (trinucleotide repeat containing 6) family of proteins have been shown to stably associate with Agos in mammalian cells. Here, we describe the isolation and functional characterization of TNRC6B- and TNRC6C-containing complexes. We show that TNRC6B and TNRC6C proteins associate with all four human Agos which are already loaded with microRNAs. Detailed domain analysis of TNRC6B protein indicated that distinct domains of the protein are required for Ago binding and P-body localization. Functional analysis using reporter constructs responsive to TNRC6B tethered through an MS2-binding domain indicates that neither the Ago-binding nor the P-body localization domains are required for translational silencing. In contrast, the C-terminal domain containing the RNA recognition motif plays a critical role in the silencing mediated by the TNRC6B protein.

scholarly journals Affinity and Structural Analysis of the U1A RNA Recognition Motif with Engineered Methionines to Improve Experimental Phasing

Crystals ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 273
Author(s):  
Yoshita Srivastava ◽  
Rachel Bonn-Breach ◽  
Sai Shashank Chavali ◽  
Geoffrey M. Lippa ◽  
Jermaine L. Jenkins ◽  
...  
Keyword(s):  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Molecular Replacement ◽  
Hydrophobic Core ◽  
Anomalous Diffraction ◽  
Recognition Motif ◽  
Determination Process ◽  
Experimental Phasing ◽  
Crystal Contacts ◽  
Apical Loop

RNA plays a central role in all organisms and can fold into complex structures to orchestrate function. Visualization of such structures often requires crystallization, which can be a bottleneck in the structure-determination process. To promote crystallization, an RNA-recognition motif (RRM) of the U1A spliceosomal protein has been co-opted as a crystallization module. Specifically, the U1-snRNA hairpin II (hpII) single-stranded loop recognized by U1A can be transplanted into an RNA target to promote crystal contacts and to attain phase information via molecular replacement or anomalous diffraction methods using selenomethionine. Herein, we produced the F37M/F77M mutant of U1A to augment the phasing capability of this powerful crystallization module. Selenomethionine-substituted U1A(F37M/F77M) retains high affinity for hpII (KD of 59.7 ± 11.4 nM). The 2.20 Å resolution crystal structure reveals that the mutated sidechains make new S-π interactions in the hydrophobic core and are useful for single-wavelength anomalous diffraction. Crystals were also attained of U1A(F37M/F77M) in complex with a bacterial preQ1-II riboswitch. The F34M/F37M/F77M mutant was introduced similarly into a lab-evolved U1A variant (TBP6.9) that recognizes the internal bulged loop of HIV-1 TAR RNA. We envision that this short RNA sequence can be placed into non-essential duplex regions to promote crystallization and phasing of target RNAs. We show that selenomethionine-substituted TBP6.9(F34M/F37M/F77M) binds a TAR variant wherein the apical loop was replaced with a GNRA tetraloop (KD of 69.8 ± 2.9 nM), laying the groundwork for use of TBP6.9(F34M/F37M/F77M) as a crystallization module. These new tools are available to the research community.

Identification and expression analysis of Dazl homologue in Cynops cyanurus

Zygote ◽  
2021 ◽  
pp. 1-6
Author(s):  
Yinjiao Zhao ◽  
Ya Du ◽  
Qinglan Ge ◽  
Fang Yan ◽  
Shu Wei
Keyword(s):  
Phylogenetic Analysis ◽  
Comparative Studies ◽  
Rna Binding ◽  
Rna Binding Protein ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Specific Expression ◽  
Recognition Motif ◽  
Deleted In Azoospermia ◽  
Specific Expression Pattern

Summary The Dazl (deleted in azoospermia-like) gene encodes an RNA-binding protein containing an RNA recognition motif (RRM) and a DAZ motif. Dazl is essential for gametogenesis in vertebrates. In this study, we report the cloning of Dazl cDNA from Cynops cyanurus. Ccdazl mRNA showed a germline-specific expression pattern as expected. Ccdazl expression gradually decreased during oogenesis, suggesting that it may be involved in oocyte development. Phylogenetic analysis revealed that the Ccdazl protein shares conserved motifs/domains with Dazl proteins from other species. Cloning of Ccdazl provides a new tool to carry out comparative studies of germ cell development in amphibians.

scholarly journals A Small Cyclic β‐Hairpin Peptide Mimics the Rbfox2 RNA Recognition Motif and Binds to the Precursor miRNA 20b

ChemBioChem ◽  
2019 ◽  
Vol 20 (7) ◽  
pp. 931-939 ◽  
Author(s):  
Yi‐Ting Sun ◽  
Matthew D. Shortridge ◽  
Gabriele Varani
Keyword(s):  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Peptide Mimics ◽  
Recognition Motif
Sign in / Sign up

Export Citation Format

Share Document