Specific interactions between Dicer-like proteins and HYL1/DRB- family dsRNA-binding proteins in Arabidopsis thaliana

2005 ◽  
Vol 57 (2) ◽  
pp. 173-188 ◽  
Author(s):  
Akihiro Hiraguri ◽  
Riku Itoh ◽  
Naoko Kondo ◽  
Yasuko Nomura ◽  
Daisuke Aizawa ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Binding Proteins ◽  
Specific Interactions ◽  
Dsrna Binding

scholarly journals The ATXN2 Orthologs CID3 and CID4, Act Redundantly to In-Fluence Developmental Pathways throughout the Life Cycle of Arabidopsis thaliana

2021 ◽  
Vol 22 (6) ◽  
pp. 3068
Author(s):  
Zaira M. López-Juárez ◽  
Laura Aguilar-Henonin ◽  
Plinio Guzmán
Keyword(s):  
Arabidopsis Thaliana ◽  
Life Cycle ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Leaf Growth ◽  
Transcriptome Profiling ◽  
Developmental Pathways ◽  
Model Organisms ◽  
Key Factors

RNA-binding proteins (RBPs) are key elements involved in post-transcriptional regulation. Ataxin-2 (ATXN2) is an evolutionarily conserved RBP protein, whose function has been studied in several model organisms, from Saccharomyces cerevisiae to the Homo sapiens. ATXN2 interacts with poly(A) binding proteins (PABP) and binds to specific sequences at the 3′UTR of target mRNAs to stabilize them. CTC-Interacting Domain3 (CID3) and CID4 are two ATXN2 orthologs present in plant genomes whose function is unknown. In the present study, phenotypical and transcriptome profiling were used to examine the role of CID3 and CID4 in Arabidopsis thaliana. We found that they act redundantly to influence pathways throughout the life cycle. cid3cid4 double mutant showed a delay in flowering time and a reduced rosette size. Transcriptome profiling revealed that key factors that promote floral transition and floral meristem identity were downregulated in cid3cid4 whereas the flowering repressor FLOWERING LOCUS C (FLC) was upregulated. Expression of key factors in the photoperiodic regulation of flowering and circadian clock pathways, were also altered in cid3cid4, as well as the expression of several transcription factors and miRNAs encoding genes involved in leaf growth dynamics. These findings reveal that ATXN2 orthologs may have a role in developmental pathways throughout the life cycle of plants.

scholarly journals Arabidopsis thaliana organelles mimic the T7 phage DNA replisome with specific interactions between Twinkle protein and DNA polymerases Pol1A and Pol1B

2019 ◽  
Vol 19 (1) ◽  
Author(s):  
Stewart A. Morley ◽  
Antolín Peralta-Castro ◽  
Luis G. Brieba ◽  
Justin Miller ◽  
Kai Li Ong ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Dna Polymerases ◽  
Specific Interactions ◽  
Phage Dna ◽  
T7 Phage

scholarly journals Cytosolic delivery of siRNA by ultra-high affinity dsRNA binding proteins

2017 ◽  
Vol 45 (13) ◽  
pp. 7602-7614 ◽  
Author(s):  
Nicole J. Yang ◽  
Monique J. Kauke ◽  
Fangdi Sun ◽  
Lucy F. Yang ◽  
Katie F. Maass ◽  
...  
Keyword(s):  
Binding Proteins ◽  
High Affinity ◽  
Cytosolic Delivery ◽  
Dsrna Binding

scholarly journals Two RNA Binding Proteins, HEN4 and HUA1, Act in the Processing of AGAMOUS Pre-mRNA in Arabidopsis thaliana

2003 ◽  
Vol 4 (1) ◽  
pp. 53-66 ◽  
Author(s):  
Yulan Cheng ◽  
Naohiro Kato ◽  
Wenming Wang ◽  
Junjie Li ◽  
Xuemei Chen
Keyword(s):  
Arabidopsis Thaliana ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins

scholarly journals PRKRA Localizes to Nuage Structures and the Ectoplasmic Specialization and Tubulobulbar Complexes in Rat and Mouse Testis

2014 ◽  
Vol 2014 ◽  
pp. 1-9
Author(s):  
Junya Suzuki ◽  
Sadaki Yokota
Keyword(s):  
Sertoli Cells ◽  
Rna Silencing ◽  
Binding Proteins ◽  
Spermatogenic Cells ◽  
P Bodies ◽  
Cytoplasmic Rna ◽  
Dsrna Binding ◽  
Chromatoid Bodies ◽  
Pachytene Spermatocytes ◽  
Ectoplasmic Specialization

The cytoplasmic RNA-induced silencing complex (RISC) contains dsRNA binding proteins, including PRKRA, TRBP, and Dicer. RISC localizes to P-bodies. The nuage of the spermatogenic cells has function similar to the P-bodies. We study whether PRKRA localizes to nuage of spermatogenic cells of rat and mouse. PRKRA localized to four types of nuage structures, including aggregates of 60–90 nm particles, irregularly-shaped perinuclear granules, and intermitochondrial cement of pachytene spermatocytes, and chromatoid bodies of round spermatids. In addition, PRKRA is associated with dense material surrounding tubulobulbar complexes and with the ectoplasmic specialization. The results suggest that PRKRA functions in the nuage as an element of RNA silencing system and plays unknown role in the ectoplasmic specialization and at the tubulobulbar complexes of Sertoli cells attaching the head of late spermatids.

Structural analysis of the C-terminal domain of the spliceosomal helicase Prp22

2012 ◽  
Vol 393 (10) ◽  
pp. 1131-1140 ◽  
Author(s):  
Denis Kudlinzki ◽  
Andreas Schmitt ◽  
Henning Christian ◽  
Ralf Ficner
Keyword(s):  
Rna Binding ◽  
Dna Helicase ◽  
Specific Interactions ◽  
Winged Helix ◽  
Dsrna Binding ◽  
Binding Surface ◽  
Rna Complexes ◽  
Positively Charged ◽  
Analogous Function

Abstract Splicing of pre-mRNA requires the activity of at least eight different DEAD/H-box proteins that are involved in distinct steps of the splicing process. These proteins are driving the spliceosomal machinery by ATP-dependent unwinding of dsRNA and/or disrupting protein-RNA complexes. The spliceosomal DEAH-box proteins Prp2, Prp16, Prp22 and Prp43 share homologous C-terminal domains (CTD). We have determined the crystal structure of the CTD of human Prp22 by means of MAD. The fold of the human Prp22-CTD closely resembles that of the yeast Prp43-CTD. The similarity of these helicase-associated CTDs to the winged-helix and ratchet domains of the DNA helicase Hel308 suggests an analogous function in dsRNA binding and unwinding. Here, we also demonstrate that the CTD has a significant impact on the ATPase activity of yPrp22 in vitro. Homology modeling of the CTDs of hPrp2, hPrp16 and hPrp43 suggests that the CTDs of spliceosomal helicases contain conserved positively charged patches on their surfaces representing a common RNA-binding surface as well as divergent regions most likely mediating specific interactions with different proteins of the spliceosome.

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