scholarly journals RNA Recognition Motif-Containing Protein ORRM4 Broadly Affects Mitochondrial RNA Editing and Impacts Plant Development and Flowering

2015 ◽  
Vol 170 (1) ◽  
pp. 294-309 ◽  
Author(s):  
Xiaowen Shi ◽  
Arnaud Germain ◽  
Maureen R. Hanson ◽  
Stéphane Bentolila
Keyword(s):  
Rna Editing ◽  
Plant Development ◽  
Rna Recognition Motif ◽  
Mitochondrial Rna ◽  
Rna Recognition ◽  
Recognition Motif

scholarly journals ORRM5, an RNA recognition motif-containing protein, has a unique effect on mitochondrial RNA editing

2017 ◽  
Vol 68 (11) ◽  
pp. 2833-2847 ◽  
Author(s):  
Xiaowen Shi ◽  
Benoit Castandet ◽  
Arnaud Germain ◽  
Maureen R Hanson ◽  
Stéphane Bentolila
Keyword(s):  
Rna Editing ◽  
Rna Recognition Motif ◽  
Mitochondrial Rna ◽  
Rna Recognition ◽  
Recognition Motif ◽  
Unique Effect

scholarly journals The RNA recognition motif protein CP33A is a global ligand of chloroplast mRNAs and is essential for plastid biogenesis and plant development

2017 ◽  
Vol 89 (3) ◽  
pp. 472-485 ◽  
Author(s):  
Marlene Teubner ◽  
Janina Fuß ◽  
Kristina Kühn ◽  
Kirsten Krause ◽  
Christian Schmitz-Linneweber
Keyword(s):  
Plant Development ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Recognition Motif

Molecular and functional diversity of organelle RNA editing mediated by RNA recognition motif‐containing protein ORRM4 in tomato

2020 ◽  
Vol 228 (2) ◽  
pp. 570-585
Author(s):  
Yongfang Yang ◽  
Xiuying Liu ◽  
Keru Wang ◽  
Jinyan Li ◽  
Guoning Zhu ◽  
...  
Keyword(s):  
Rna Editing ◽  
Functional Diversity ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Recognition Motif

scholarly journals Two organelle RNA recognition motif proteins affect distinct sets of RNA editing sites in the Arabidopsis thaliana plastid

Plant Direct ◽  
2020 ◽  
Vol 4 (4) ◽  
Author(s):  
Audrey M. Searing ◽  
Manasa B. Satyanarayan ◽  
James P. O′Donnell ◽  
Yan Lu
Keyword(s):  
Arabidopsis Thaliana ◽  
Rna Editing ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Recognition Motif

scholarly journals An RNA recognition motif-containing protein is required for plastid RNA editing in Arabidopsis and maize

2013 ◽  
Vol 110 (12) ◽  
pp. E1169-E1178 ◽  
Author(s):  
T. Sun ◽  
A. Germain ◽  
L. Giloteaux ◽  
K. Hammani ◽  
A. Barkan ◽  
...  
Keyword(s):  
Rna Editing ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Recognition Motif

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.

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