scholarly journals Interaction modulation through arrays of clustered methyl-arginine protein modifications

2018 ◽  
Vol 1 (5) ◽  
pp. e201800178 ◽  
Author(s):  
Jonathan Woodsmith ◽  
Victoria Casado-Medrano ◽  
Nouhad Benlasfer ◽  
Rebecca L Eccles ◽  
Saskia Hutten ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Structural Complexity ◽  
Arginine Methylation ◽  
Cellular Interactions ◽  
Post Translational Modification ◽  
Systematic Analysis ◽  
Interacting Protein ◽  
Cytoplasmic Rna ◽  
Interaction Interface

Systematic analysis of human arginine methylation identifies two distinct signaling modes; either isolated modifications akin to canonical post-translational modification regulation, or clustered arrays within disordered protein sequence. Hundreds of proteins contain these methyl-arginine arrays and are more prone to accumulate mutations and more tightly expression-regulated than dispersed methylation targets. Arginines within an array in the highly methylated RNA-binding protein synaptotagmin binding cytoplasmic RNA interacting protein (SYNCRIP) were experimentally shown to function in concert, providing a tunable protein interaction interface. Quantitative immunoprecipitation assays defined two distinct cumulative binding mechanisms operating across 18 proximal arginine–glycine (RG) motifs in SYNCRIP. Functional binding to the methyltransferase PRMT1 was promoted by continual arginine stretches, whereas interaction with the methyl-binding protein SMN1 was arginine content–dependent irrespective of linear position within the unstructured region. This study highlights how highly repetitive modifiable amino acid arrays in low structural complexity regions can provide regulatory platforms, with SYNCRIP as an extreme example how arginine methylation leverages these disordered sequences to mediate cellular interactions.

scholarly journals Interaction modulation through arrays of clustered methyl-arginine protein modifications

2018 ◽  
Author(s):  
Jonathan Woodsmith ◽  
Victoria Casado-Medrano ◽  
Nouhad Benlasfer ◽  
Rebecca L. Eccles ◽  
Saskia Hutten ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Structural Complexity ◽  
Arginine Methylation ◽  
Cellular Interactions ◽  
Systematic Analysis ◽  
Methyl Transferase ◽  
Disordered Protein ◽  
Interaction Interface ◽  
Binding Mechanisms

AbstractSystematic analysis of human arginine methylation identifies two distinct signaling modes; either isolated modifications akin to canonical PTM regulation, or clustered arrays within disordered protein sequence. Hundreds of proteins contain these methyl-arginine arrays and are more prone to accumulate mutations and more tightly expression-regulated than dispersed methylation targets. Arginines within an array in the highly methylated RNA binding protein SYNCRIP were experimentally shown to function in concert providing a tunable protein interaction interface. Quantitative immuno-precipitation assays defined two distinct cumulative binding mechanisms operating across 18 proximal arginine-glycine (RG) motifs in SYNCRIP. Functional binding to the methyl-transferase PRMT1 was promoted by continual arginine stretches while interaction with the methyl-binding protein SMN1 was arginine content dependent irrespective of linear position within the unstructured region. This study highlights how highly-repetitive modifiable amino acid arrays in low structural complexity regions can provide regulatory platforms, with SYNCRIP as an extreme example how arginine methylation leverages these disordered sequences to mediate cellular interactions.

AtGRP2, a cold-induced nucleo-cytoplasmic RNA-binding protein, has a role in flower and seed development

Planta ◽  
2006 ◽  
Vol 225 (6) ◽  
pp. 1339-1351 ◽  
Author(s):  
Adriana Flores Fusaro ◽  
Silvia Nora Bocca ◽  
Rose Lucia Braz Ramos ◽  
Rosa Maria Barrôco ◽  
Claudia Magioli ◽  
...  
Keyword(s):  
Seed Development ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Cytoplasmic Rna

The RNA-binding protein FUS/TLS is a common aggregate-interacting protein in polyglutamine diseases

2010 ◽  
Vol 66 (1) ◽  
pp. 131-133 ◽  
Author(s):  
Hiroshi Doi ◽  
Shigeru Koyano ◽  
Yume Suzuki ◽  
Nobuyuki Nukina ◽  
Yoshiyuki Kuroiwa
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Polyglutamine Diseases ◽  
Interacting Protein

scholarly journals Dynamic regulation of immunity through post-translational control of defense transcript splicing

2019 ◽  
Author(s):  
Keini Dressano ◽  
Philipp R Weckwerth ◽  
Elly Poretsky ◽  
Yohei Takahashi ◽  
Carleen Villarreal ◽  
...  
Keyword(s):  
Immune Responses ◽  
Translational Control ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Negative Regulator ◽  
Signaling Proteins ◽  
Receptor Signaling ◽  
Post Translational Modification ◽  
Defense Signaling

AbstractSurvival of all living organisms requires the ability to detect attack and swiftly counter with protective immune responses. Despite considerable mechanistic advances, interconnectivity of signaling circuits often remains unclear. A newly-characterized protein, IMMUNOREGULATORY RNA-BINDING PROTEIN (IRR), negatively regulates immune responses in both maize and Arabidopsis, with disrupted function resulting in enhanced disease resistance. IRR physically interacts with, and promotes canonical splicing of, transcripts encoding defense signaling proteins, including the key negative regulator of pattern recognition receptor signaling complexes, CALCIUM-DEPENDENT PROTEIN KINASE 28 (CPK28). Upon immune activation by Plant Elicitor Peptides (Peps), IRR is dephosphorylated, disrupting interaction withCPK28transcripts and resulting in accumulation of an alternative splice variant encoding a truncated CPK28 protein with impaired kinase activity and diminished function as a negative regulator. We demonstrate a novel circuit linking Pep-induced post-translational modification of IRR with post-transcriptionally-mediated attenuation of CPK28 function to dynamically amplify Pep signaling and immune output.One Sentence SummaryPlant innate immunity is promoted by post-translational modification of a novel RNA-binding protein that regulates alternative splicing of transcripts encoding defense signaling proteins to dynamically increase immune receptor signaling capacity through deactivation of a key signal-buffering circuit.

At the Interface of Three Nucleic Acids: The Role of RNA-Binding Proteins and Poly(ADP-ribose) in DNA Repair

Acta Naturae ◽  
2017 ◽  
Vol 9 (2) ◽  
pp. 4-16 ◽  
Author(s):  
E. E. Alemasova ◽  
O. I. Lavrik
Keyword(s):  
Dna Damage ◽  
Dna Repair ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Binding Protein ◽  
Regulation Of Gene Expression ◽  
Rna Granules ◽  
Dna And Rna ◽  
Cytoplasmic Rna

RNA-binding proteins (RBPs) regulate RNA metabolism, from synthesis to decay. When bound to RNA, RBPs act as guardians of the genome integrity at different levels, from DNA damage prevention to the post-transcriptional regulation of gene expression. Recently, RBPs have been shown to participate in DNA repair. This fact is of special interest as DNA repair pathways do not generally involve RNA. DNA damage in higher organisms triggers the formation of the RNA-like polymer - poly(ADP-ribose) (PAR). Nucleic acid-like properties allow PAR to recruit DNA- and RNA-binding proteins to the site of DNA damage. It is suggested that poly(ADP-ribose) and RBPs not only modulate the activities of DNA repair factors, but that they also play an important role in the formation of transient repairosome complexes in the nucleus. Cytoplasmic biomolecules are subjected to similar sorting during the formation of RNA assemblages by functionally related mRNAs and promiscuous RBPs. The Y-box-binding protein 1 (YB-1) is the major component of cytoplasmic RNA granules. Although YB-1 is a classic RNA-binding protein, it is now regarded as a non-canonical factor of DNA repair.

scholarly journals A Novel Double-stranded RNA-binding Protein, Disco Interacting Protein 1 (DIP1), Contributes to Cell Fate Decisions duringDrosophilaDevelopment

2003 ◽  
Vol 278 (39) ◽  
pp. 38040-38050 ◽  
Author(s):  
Dorothy DeSousa ◽  
Mahua Mukhopadhyay ◽  
Peter Pelka ◽  
Xiaoli Zhao ◽  
Bijan K. Dey ◽  
...  
Keyword(s):  
Cell Fate ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Interacting Protein ◽  
Double Stranded Rna ◽  
Cell Fate Decisions
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