scholarly journals Small RNA sequencing of Potato leafroll virus-infected plants reveals an additional subgenomic RNA encoding a sequence-specific RNA-binding protein

Virology ◽  
2013 ◽  
Vol 438 (2) ◽  
pp. 61-69 ◽  
Author(s):  
Yeen Ting Hwang ◽  
Melanie Kalischuk ◽  
Adriana F. Fusaro ◽  
Peter M. Waterhouse ◽  
Lawrence Kawchuk
Keyword(s):  
Rna Sequencing ◽  
Small Rna ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Potato Leafroll Virus ◽  
Small Rna Sequencing ◽  
Subgenomic Rna ◽  
Leafroll Virus

scholarly journals RNA-Binding Protein MSI2 Binds to miR-301a-3p and Facilitates Its Distribution in Mitochondria of Endothelial Cells

2021 ◽  
Vol 7 ◽  
Author(s):  
Qian Qian Guo ◽  
Jing Gao ◽  
Xiao Wei Wang ◽  
Xian Lun Yin ◽  
Shu Cui Zhang ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Rna Binding ◽  
Binding Protein ◽  
Umbilical Vein ◽  
Quantitative Polymerase Chain Reaction ◽  
Rna Binding Protein ◽  
Small Rna Sequencing ◽  
Valuable Insight ◽  
Label Free ◽  
Mitochondrial Distribution

Numerous miRNAs have been detected in mitochondria, which play important roles in many physiological and pathophysiological processes. However, the dynamic changes of miRNA distribution in mitochondria and their mechanisms in reactive oxygen species (ROS)-induced endothelial injury remain unclear. Therefore, miRNA levels in whole cells and mitochondria of H2O2-treated endothelial cells were analyzed by small RNA sequencing in the present study. The results showed that H2O2 significantly reduced the relative mitochondrial distribution of dozens of miRNAs in human umbilical vein endothelial cells (HUVECs). Among the high-abundance miRNAs, miR-301a-3p has the most significant changes in the redistribution between cytosol and mitochondria confirmed by absolute quantitative polymerase chain reaction (qPCR). To unravel the mechanism of miR-301a-3p distribution in mitochondria, RNA pull-down followed by label-free quantitative proteomic analysis was performed, and RNA-binding protein Musashi RNA binding protein 2 (MSI2) was found to specifically bind to miR-301a-3p. Western blotting and immunofluorescence colocalization assay showed that MSI2 was located in mitochondria of various cell types. H2O2 significantly downregulated MSI2 expression in whole endothelial cells, promoted the distribution of MSI2 in cytosol and decreased its distribution in the mitochondria. Moreover, overexpression of MSI2 increased the mitochondrial distribution of miR-301a-3p, whereas inhibition of MSI2 decreased its distribution in mitochondria. Thus, MSI2 might be responsible for the distribution of miR-301a-3p between cytosol and mitochondria in endothelial cells. Our findings revealed for the first time that MSI2 was involved in the regulation of miRNA distribution in mitochondria and provided valuable insight into the mechanism of mitochondrial distribution of miRNAs.

Structure and subcellular localization of a small RNA-binding protein from tobacco

1997 ◽  
Vol 12 (1) ◽  
pp. 215-221 ◽  
Author(s):  
Kazuki Moriguchi ◽  
Mamoru Sugita ◽  
Masahiro Sugiura
Keyword(s):  
Subcellular Localization ◽  
Small Rna ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein

The cellular RNA-binding protein EAP recognizes a conserved stem-loop in the Epstein-Barr virus small RNA EBER 1

1993 ◽  
Vol 13 (1) ◽  
pp. 703-710
Author(s):  
D P Toczyski ◽  
J A Steitz
Keyword(s):  
Fusion Protein ◽  
Small Rna ◽  
Epstein Barr Virus ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Glutathione S Transferase ◽  
Stem Loop ◽  
Barr Virus ◽  
Epstein Barr

EAP (EBER-associated protein) is an abundant, 15-kDa cellular RNA-binding protein which associates with certain herpesvirus small RNAs. We have raised polyclonal anti-EAP antibodies against a glutathione S-transferase-EAP fusion protein. Analysis of the RNA precipitated by these antibodies from Epstein-Barr virus (EBV)- or herpesvirus papio (HVP)-infected cells shows that > 95% of EBER 1 (EBV-encoded RNA 1) and the majority of HVP 1 (an HVP small RNA homologous to EBER 1) are associated with EAP. RNase protection experiments performed on native EBER 1 particles with affinity-purified anti-EAP antibodies demonstrate that EAP binds a stem-loop structure (stem-loop 3) of EBER 1. Since bacterially expressed glutathione S-transferase-EAP fusion protein binds EBER 1, we conclude that EAP binding is independent of any other cellular or viral protein. Detailed mutational analyses of stem-loop 3 suggest that EAP recognizes the majority of the nucleotides in this hairpin, interacting with both single-stranded and double-stranded regions in a sequence-specific manner. Binding studies utilizing EBER 1 deletion mutants suggest that there may also be a second, weaker EAP-binding site on stem-loop 4 of EBER 1. These data and the fact that stem-loop 3 represents the most highly conserved region between EBER 1 and HVP 1 suggest that EAP binding is a critical aspect of EBER 1 and HVP 1 function.

OsDEG10 encoding a small RNA-binding protein is involved in abiotic stress signaling

2009 ◽  
Vol 380 (3) ◽  
pp. 597-602 ◽  
Author(s):  
Hee-Yeon Park ◽  
In Soon Kang ◽  
Ji-Sung Han ◽  
Choon-Hwan Lee ◽  
Gynheung An ◽  
...  
Keyword(s):  
Abiotic Stress ◽  
Small Rna ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Stress Signaling

scholarly journals Systemic delivery of siRNA in pumpkin by a plant PHLOEM SMALL RNA-BINDING PROTEIN 1-ribonucleoprotein complex

2014 ◽  
Vol 80 (4) ◽  
pp. 683-694 ◽  
Author(s):  
Byung-Kook Ham ◽  
Gang Li ◽  
Weitao Jia ◽  
Julie A. Leary ◽  
William J. Lucas
Keyword(s):  
Small Rna ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Systemic Delivery ◽  
Ribonucleoprotein Complex

scholarly journals The cellular RNA-binding protein EAP recognizes a conserved stem-loop in the Epstein-Barr virus small RNA EBER 1.

1993 ◽  
Vol 13 (1) ◽  
pp. 703-710 ◽  
Author(s):  
D P Toczyski ◽  
J A Steitz
Keyword(s):  
Fusion Protein ◽  
Small Rna ◽  
Epstein Barr Virus ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Glutathione S Transferase ◽  
Stem Loop ◽  
Barr Virus ◽  
Epstein Barr

EAP (EBER-associated protein) is an abundant, 15-kDa cellular RNA-binding protein which associates with certain herpesvirus small RNAs. We have raised polyclonal anti-EAP antibodies against a glutathione S-transferase-EAP fusion protein. Analysis of the RNA precipitated by these antibodies from Epstein-Barr virus (EBV)- or herpesvirus papio (HVP)-infected cells shows that > 95% of EBER 1 (EBV-encoded RNA 1) and the majority of HVP 1 (an HVP small RNA homologous to EBER 1) are associated with EAP. RNase protection experiments performed on native EBER 1 particles with affinity-purified anti-EAP antibodies demonstrate that EAP binds a stem-loop structure (stem-loop 3) of EBER 1. Since bacterially expressed glutathione S-transferase-EAP fusion protein binds EBER 1, we conclude that EAP binding is independent of any other cellular or viral protein. Detailed mutational analyses of stem-loop 3 suggest that EAP recognizes the majority of the nucleotides in this hairpin, interacting with both single-stranded and double-stranded regions in a sequence-specific manner. Binding studies utilizing EBER 1 deletion mutants suggest that there may also be a second, weaker EAP-binding site on stem-loop 4 of EBER 1. These data and the fact that stem-loop 3 represents the most highly conserved region between EBER 1 and HVP 1 suggest that EAP binding is a critical aspect of EBER 1 and HVP 1 function.

scholarly journals RelA protein stimulates the activity of RyhB small RNA by acting on RNA-binding protein Hfq

2012 ◽  
Vol 109 (12) ◽  
pp. 4621-4626 ◽  
Author(s):  
L. Argaman ◽  
M. Elgrably-Weiss ◽  
T. Hershko ◽  
J. Vogel ◽  
S. Altuvia
Keyword(s):  
Small Rna ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein
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