scholarly journals Expression of phage P4 integrase is regulated negatively by both Int and Vis

2006 ◽  
Vol 87 (8) ◽  
pp. 2423-2431 ◽  
Author(s):  
D. Piazzolla ◽  
S. Calì ◽  
E. Spoldi ◽  
F. Forti ◽  
C. Sala ◽  
...  
Keyword(s):  
Rna Binding ◽  
Transcription Termination ◽  
Rna Binding Protein ◽  
Mrna Degradation ◽  
Negative Regulation ◽  
The Other ◽  
Terminal Portion ◽  
N Terminus ◽  
Different Levels ◽  
Complex Manner

Phage P4 int gene encodes the integrase responsible for phage integration into and excision from the Escherichia coli chromosome. Here, the data showing that P4 int expression is regulated in a complex manner at different levels are presented. First of all, the Pint promoter is regulated negatively by both Int and Vis, the P4 excisionase. The N-terminal portion of Int appears to be sufficient for such a negative autoregulation, suggesting that the Int N terminus is implicated in DNA binding. Second, full-length transcripts covering the entire int gene could be detected only upon P4 infection, whereas in P4 lysogens only short 5′-end covering transcripts were detectable. On the other hand, transcripts covering the 5′-end of int were also very abundant upon infection. It thus appears that premature transcription termination and/or mRNA degradation play a role in Int-negative regulation both on the basal prophage transcription and upon infection. Finally, comparison between Pint–lacZ transcriptional and translational fusions suggests that Vis regulates Int expression post-transcriptionally. The findings that Vis is also an RNA-binding protein and that Int may be translated from two different start codons have implications on possible regulation models of Int expression.

scholarly journals Negative regulation of RNA-binding protein HuR by tumor-suppressor ECRG2

Oncogene ◽  
2015 ◽  
Vol 35 (20) ◽  
pp. 2565-2573 ◽  
Author(s):  
C Lucchesi ◽  
M S Sheikh ◽  
Y Huang
Keyword(s):  
Tumor Suppressor ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Negative Regulation

scholarly journals A yeast RNA-binding protein shuttles between the nucleus and the cytoplasm.

1994 ◽  
Vol 14 (12) ◽  
pp. 8399-8407 ◽  
Author(s):  
J Flach ◽  
M Bossie ◽  
J Vogel ◽  
A Corbett ◽  
T Jinks ◽  
...  
Keyword(s):  
Nuclear Protein ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Rna Binding Protein ◽  
Wild Type ◽  
Yeast Saccharomyces Cerevisiae ◽  
Binding Motifs ◽  
C Terminus ◽  
N Terminus ◽  
Heterogeneous Nuclear Ribonucleoproteins

RNA-binding proteins have been suggested to move in association with RNA as it leaves the nucleus. The NPL3 gene of the yeast Saccharomyces cerevisiae encodes in nuclear protein with consensus RNA-binding motifs and similarity to heterogeneous nuclear ribonucleoproteins and members of the S/R protein family. We show that although Npl3 is located in the nucleus, it can shuttle between nuclei in yeast heterokaryons. In contrast, other nucleus-targeted proteins do not leave the nucleus under similar conditions. Mutants missing the RNA-binding motifs or the N terminus are still capable of shuttling in and out of the nucleus. Npl3 mutants missing the C terminus fail to localize to the nucleus. Overproduction of Npl3 in wild-type cells shows cell growth. This toxicity depends on the presence of series of unique repeats in the N terminus and localization to the nucleus. We suggest that the properties of Npl3 are consistent with it being involved in export of RNAs from the nucleus.

scholarly journals Unique repression domains of Pumilio utilize deadenylation and decapping factors to accelerate destruction of target mRNAs

2019 ◽  
Vol 48 (4) ◽  
pp. 1843-1871 ◽  
Author(s):  
René M Arvola ◽  
Chung-Te Chang ◽  
Joseph P Buytendorp ◽  
Yevgen Levdansky ◽  
Eugene Valkov ◽  
...  
Keyword(s):  
Stem Cell ◽  
Catalytic Activity ◽  
Protein Expression ◽  
Cell Fate ◽  
Rna Binding ◽  
Rna Binding Protein ◽  
Stem Cell Fate ◽  
Target Mrnas ◽  
N Terminus ◽  
Decapping Enzyme

Abstract Pumilio is an RNA-binding protein that represses a network of mRNAs to control embryogenesis, stem cell fate, fertility and neurological functions in Drosophila. We sought to identify the mechanism of Pumilio-mediated repression and find that it accelerates degradation of target mRNAs, mediated by three N-terminal Repression Domains (RDs), which are unique to Pumilio orthologs. We show that the repressive activities of the Pumilio RDs depend on specific subunits of the Ccr4–Not (CNOT) deadenylase complex. Depletion of Pop2, Not1, Not2, or Not3 subunits alleviates Pumilio RD-mediated repression of protein expression and mRNA decay, whereas depletion of other CNOT components had little or no effect. Moreover, the catalytic activity of Pop2 deadenylase is important for Pumilio RD activity. Further, we show that the Pumilio RDs directly bind to the CNOT complex. We also report that the decapping enzyme, Dcp2, participates in repression by the N-terminus of Pumilio. These results support a model wherein Pumilio utilizes CNOT deadenylase and decapping complexes to accelerate destruction of target mRNAs. Because the N-terminal RDs are conserved in mammalian Pumilio orthologs, the results of this work broadly enhance our understanding of Pumilio function and roles in diseases including cancer, neurodegeneration and epilepsy.

scholarly journals A yeast RNA-binding protein shuttles between the nucleus and the cytoplasm

1994 ◽  
Vol 14 (12) ◽  
pp. 8399-8407
Author(s):  
J Flach ◽  
M Bossie ◽  
J Vogel ◽  
A Corbett ◽  
T Jinks ◽  
...  
Keyword(s):  
Nuclear Protein ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Rna Binding Protein ◽  
Wild Type ◽  
Yeast Saccharomyces Cerevisiae ◽  
Binding Motifs ◽  
C Terminus ◽  
N Terminus ◽  
Heterogeneous Nuclear Ribonucleoproteins

RNA-binding proteins have been suggested to move in association with RNA as it leaves the nucleus. The NPL3 gene of the yeast Saccharomyces cerevisiae encodes in nuclear protein with consensus RNA-binding motifs and similarity to heterogeneous nuclear ribonucleoproteins and members of the S/R protein family. We show that although Npl3 is located in the nucleus, it can shuttle between nuclei in yeast heterokaryons. In contrast, other nucleus-targeted proteins do not leave the nucleus under similar conditions. Mutants missing the RNA-binding motifs or the N terminus are still capable of shuttling in and out of the nucleus. Npl3 mutants missing the C terminus fail to localize to the nucleus. Overproduction of Npl3 in wild-type cells shows cell growth. This toxicity depends on the presence of series of unique repeats in the N terminus and localization to the nucleus. We suggest that the properties of Npl3 are consistent with it being involved in export of RNAs from the nucleus.

scholarly journals An mRNA silencing mechanism reliant on the cooperation between REGE-1/Regnase-1 and RLE-1/Roquin-1

2021 ◽  
Author(s):  
Daria Sobanska ◽  
Alicja A Komur ◽  
Agnieszka Chabowska-Kita ◽  
Julita Gumna ◽  
Pooja Kumari ◽  
...  
Keyword(s):  
Functional Relationship ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
The Other ◽  
Immune Homeostasis ◽  
C Elegans ◽  
Evolutionarily Conserved ◽  
Competing Models

Regnase-1 is an evolutionarily conserved endoribonuclease, degrading diverse mRNAs important, among others, for immune homeostasis, development, and cancer. There are two competing models of Regnase-1 mediated mRNA silencing. One model postulates that Regnase-1 works together with another RNA-binding protein, Roquin-1. The other model proposes that the two proteins function separately. Studying the C. elegans Regnase-1 ortholog, REGE-1, we have uncovered a functional relationship between REGE-1 and the nematode counterpart of Roquin-1, RLE-1. While REGE-1 and RLE-1 associate with mRNA independently of each other, both proteins are essential for mRNA silencing. Intriguingly, the functional interdependence between REGE-1 and RLE-1 is reminiscent of the proposed cooperation between mammalian Regnase-1 and Roquin-1, which may underlie a prototypic silencing mechanism involving both proteins.

scholarly journals MicroRNA-466l Upregulates IL-10 Expression in TLR-Triggered Macrophages by Antagonizing RNA-Binding Protein Tristetraprolin-Mediated IL-10 mRNA Degradation

2010 ◽  
Vol 184 (11) ◽  
pp. 6053-6059 ◽  
Author(s):  
Feng Ma ◽  
Xingguang Liu ◽  
Dong Li ◽  
Pin Wang ◽  
Nan Li ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Mrna Degradation

scholarly journals Unique repression domains of Pumilio utilize deadenylation and decapping factors to accelerate destruction of target mRNAs

2019 ◽  
Author(s):  
René M. Arvola ◽  
Chung-Te Chang ◽  
Joseph P. Buytendorp ◽  
Yevgen Levdansky ◽  
Eugene Valkov ◽  
...  
Keyword(s):  
Stem Cell ◽  
Catalytic Activity ◽  
Protein Expression ◽  
Cell Fate ◽  
Rna Binding ◽  
Rna Binding Protein ◽  
Stem Cell Fate ◽  
Target Mrnas ◽  
N Terminus ◽  
Decapping Enzyme

ABSTRACTPumilio is an RNA-binding protein that represses a network of mRNAs to control embryogenesis, stem cell fate, fertility, and neurological functions in Drosophila. We sought to identify the mechanism of Pumilio-mediated repression and find that it accelerates degradation of target mRNAs, mediated by three N-terminal Repression Domains (RDs), which are unique to Pumilio orthologs. We show that the repressive activities of the Pumilio RDs depend on specific subunits of the Ccr4-Not (CNOT) deadenylase complex. Depletion of Pop2, Not1, Not2, or Not3 subunits alleviates Pumilio RD-mediated repression of protein expression and mRNA decay, whereas depletion of other CNOT components had little or no effect. Moreover, the catalytic activity of Pop2 deadenylase is important for Pumilio RD activity. Further, we show that the Pumilio RDs directly bind to the CNOT complex. We also report that the decapping enzyme, Dcp2, participates in repression by the N-terminus of Pumilio. These results support a model wherein Pumilio utilizes CNOT deadenylase and decapping complexes to accelerate destruction of target mRNAs. Because the N-terminal RDs are conserved in mammalian Pumilio orthologs, the results of this work broadly enhance our understanding of Pumilio function and roles in diseases including cancer, neurodegeneration, and epilepsy.

scholarly journals Modulation of Phase Separation by RNA: A Glimpse on N6-Methyladenosine Modification

2021 ◽  
Vol 9 ◽  
Author(s):  
Yingfeng Su ◽  
Yasen Maimaitiyiming ◽  
Lingfang Wang ◽  
Xiaodong Cheng ◽  
Chih-Hung Hsu
Keyword(s):  
Phase Separation ◽  
Driving Force ◽  
Rna Binding ◽  
Rna Binding Protein ◽  
The Other ◽  
Biological Processes ◽  
Essential Component ◽  
Modulated Phase ◽  
New Perspective ◽  
Cellular Components

Phase separation is the driving force behind formation of various biomolecular condensates (BioMCs), which sub-compartmentalize certain cellular components in a membraneless manner to orchestrate numerous biological processes. Many BioMCs are composed of proteins and RNAs. While the features and functions of proteins are well studied, less attention was paid to the other essential component RNAs. Here, we describe how RNA contributes to the biogenesis, dissolution, and properties of BioMCs as a multivalence providing scaffold for proteins/RNA to undergo phase separation. Specifically, we focus on N6-methyladenosine (m6A), the most widely distributed dynamic post-transcriptional modification, which would change the charge, conformation, and RNA-binding protein (RBP) anchoring of modified RNA. m6A RNA-modulated phase separation is a new perspective to illustrate m6A-mediated various biological processes. We summarize m6A main functions as “beacon” to recruit reader proteins and “structural switcher” to alter RNA–protein and RNA–RNA interactions to modulate phase separation and regulate the related biological processes.

scholarly journals Pat1 Contains Distinct Functional Domains That Promote P-Body Assembly and Activation of Decapping

2007 ◽  
Vol 28 (4) ◽  
pp. 1298-1312 ◽  
Author(s):  
Guy R. Pilkington ◽  
Roy Parker
Keyword(s):  
Rna Binding ◽  
Rna Binding Protein ◽  
Mrna Degradation ◽  
Functional Domains ◽  
Mrna Decapping ◽  
P Bodies ◽  
Domain Specific ◽  
Translation Repression ◽  
Functional Analyses ◽  
Multiple Stages

ABSTRACT The control of mRNA degradation and translation are important aspects of gene regulation. Recent results suggest that translation repression and mRNA decapping can be intertwined and involve the formation of a quiescent mRNP, which can accumulate in cytoplasmic foci referred to as P bodies. The Pat1 protein is a key component of this complex and an important activator of decapping, yet little is known about its function. In this work, we analyze Pat1 in Saccharomyces cerevisiae function by deletion and functional analyses. Our results identify two primary functional domains in Pat1: one promoting translation repression and P-body assembly and a second domain promoting mRNA decapping after assembly of the mRNA into a P-body mRNP. In addition, we provide evidence that Pat1 binds RNA and has numerous domain-specific interactions with mRNA decapping factors. These results indicate that Pat1 is an RNA binding protein and a multidomain protein that functions at multiple stages in the process of translation repression and mRNA decapping.

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