scholarly journals RNA Binding Protein-Mediated Post-Transcriptional Gene Regulation in Medulloblastoma

2014 ◽  
Vol 37 (5) ◽  
pp. 357-364 ◽  
Author(s):  
Rebecca Bish ◽  
Christine Vogel
Keyword(s):  
Gene Regulation ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Transcriptional Gene Regulation

Chitin binding protein as a possible RNA binding protein in Leishmania parasites

2020 ◽  
Vol 78 (1) ◽  
Author(s):  
Sajad Rashidi ◽  
Kurosh Kalantar ◽  
Celia Fernandez-Rubio ◽  
Enayat Anvari ◽  
Paul Nguewa ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Novel Proteins ◽  
Transcriptional Gene Regulation ◽  
Chitin Binding Protein ◽  
Effective Drugs ◽  
Genus Leishmania ◽  
Leishmania Parasites

ABSTRACT Leishmaniasis includes a broad spectrum of pathological outcomes in humans caused by protozoan parasites from the genus Leishmania. In recent years, proteomic techniques have introduced novel proteins with critical functions in Leishmania parasites. Based on our report of a Chitin binding protein (CBP) in our previous immunoproteomic study, this article suggests that CBP might be an RNA binding protein (RBP) in Leishmania parasites. RBPs, as key regulatory factors, have a role in post-transcriptional gene regulation. The presence of RBPs in Leishmania parasites has not been considered so far; however, this study aims to open a new venue regarding RBPs in Leishmania parasites. Confirming CBP as an RBP in Leishmania parasites, exploring other RBPs and their functions might lead to interesting issues in leishmaniasis. In fact, due to the regulatory role of RBPs in different diseases including cancers and their further classification as therapeutic targets, the emerging evaluation of CBP and RBPs from Leishmania parasites may allow the discovery of novel and effective drugs against leishmaniasis.

scholarly journals Role of the RNA-Binding Protein Tristetraprolin in Glucocorticoid-Mediated Gene Regulation

2008 ◽  
Vol 180 (12) ◽  
pp. 8342-8353 ◽  
Author(s):  
Faoud T. Ishmael ◽  
Xi Fang ◽  
Maria Rosaria Galdiero ◽  
Ulus Atasoy ◽  
William F. C. Rigby ◽  
...  
Keyword(s):  
Gene Regulation ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein

scholarly journals S1-Domain RNA-Binding Protein (CvfD) Is a New Post-Transcriptional Regulator That Mediates Cold Sensitivity, Phosphate Transport, and Virulence in Streptococcus pneumoniae D39

2020 ◽  
Author(s):  
Dhriti Sinha ◽  
Jiaqi J. Zheng ◽  
Ho-Ching Tiffany Tsui ◽  
John D. Richardson ◽  
Nicholas R. De Lay ◽  
...  
Keyword(s):  
Gene Regulation ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Rna Binding Protein ◽  
Phosphate Transport ◽  
Cold Sensitivity ◽  
Rna Biology ◽  
Transcriptional Gene Regulation ◽  
Pleiotropic Regulator

ABSTRACTPost-transcriptional gene regulation often involves RNA-binding proteins that modulate mRNA translation and/or stability either directly through protein-RNA interactions or indirectly by facilitating the annealing of small regulatory RNAs (sRNAs). The human pathogen Streptococcus pneumoniae D39 (pneumococcus) does not encode homologs to RNA-binding proteins known to be involved in promoting sRNA stability and function, such as Hfq or ProQ, even though it contains genes for at least 112 sRNAs. However, the pneumococcal genome contains genes for other RNA-binding proteins, including at least six S1-domain proteins; ribosomal protein S1 (rpsA), polynucleotide phosphorylase (pnpA), RNase R (rnr), and three proteins of unknown functions. Here, we characterize the function of one of these conserved, yet uncharacterized S1-domain proteins, SPD_1366, which we have renamed CvfD (Conserved virulence factor D), since loss of this protein results in an attenuation of virulence in a murine pneumonia model. We report that deletion of cvfD impacts expression of 144 transcripts including the pst1 operon, encoding the phosphate transport system 1 in S. pneumoniae. We further show that CvfD post-transcriptionally regulates the PhoU2 master regulator of the pneumococcal dual phosphate transport system by binding phoU2 mRNA and impacting PhoU2 translation. CvfD not only controls expression of phosphate transporter genes, but also functions as a pleiotropic regulator that impacts cold sensitivity and the expression of sRNAs and genes involved in diverse cellular functions, including manganese uptake and zinc efflux. Together, our data show that CvfD exerts a broad impact on pneumococcal physiology and virulence, partly by post-transcriptional gene regulation.SIGNIFICANCERecent advances have led to the identification of numerous sRNAs in the major human respiratory pathogen, S. pneumoniae. However, little is known about the functions of most sRNAs or RNA-binding proteins involved in RNA biology in pneumococcus. In this paper, we characterize the phenotypes and one target of the S1-domain RNA-binding protein CvfD, a homolog of “general-stress protein 13” identified, but not extensively characterized in other Firmicute species. Pneumococcal CvfD is a broadly pleiotropic regulator, whose absence results in misregulation of divalent cation homeostasis, reduced translation of the PhoU2 master regulator of phosphate uptake, altered metabolism and sRNA amounts, cold sensitivity, and attenuation of virulence. These findings underscore the critical roles of RNA biology in pneumococcal physiology and virulence.

scholarly journals Staufen1 and UPF1 exert opposite actions on the replacement of the nuclear cap-binding complex by eIF4E at the 5′ end of mRNAs

2019 ◽  
Vol 47 (17) ◽  
pp. 9313-9328 ◽  
Author(s):  
Kwon Jeong ◽  
Incheol Ryu ◽  
Joori Park ◽  
Hyun Jung Hwang ◽  
Hongseok Ha ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Functional Importance ◽  
Double Stranded Rna ◽  
Importin Α ◽  
Cap Binding Complex ◽  
Nonsense Mediated Mrna Decay ◽  
Cellular Apoptosis ◽  
Transcriptional Gene Regulation

Abstract Newly synthesized mRNAs are exported from the nucleus to cytoplasm with a 5′-cap structure bound by the nuclear cap-binding complex (CBC). During or after export, the CBC should be properly replaced by cytoplasmic cap-binding protein eIF4E for efficient protein synthesis. Nonetheless, little is known about how the replacement takes place. Here, we show that double-stranded RNA-binding protein staufen1 (STAU1) promotes efficient replacement by facilitating an association between the CBC–importin α complex and importin β. Our transcriptome-wide analyses and artificial tethering experiments also reveal that the replacement occurs more efficiently when an mRNA associates with STAU1. This event is inhibited by a key nonsense-mediated mRNA decay factor, UPF1, which directly interacts with STAU1. Furthermore, we find that cellular apoptosis that is induced by ionizing radiation is accompanied by inhibition of the replacement via increased association between STAU1 and hyperphosphorylated UPF1. Altogether, our data highlight the functional importance of STAU1 and UPF1 in the course of the replacement of the CBC by eIF4E, adding a previously unappreciated layer of post-transcriptional gene regulation.

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