Identification of target mRNAs for the clock-controlled RNA-binding protein Chlamy 1 from Chlamydomonas reinhardtii

2001 ◽  
Vol 265 (1) ◽  
pp. 180-188 ◽  
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Target Mrnas

scholarly journals RNA–Binding Protein HuD as a Versatile Factor in Neuronal and Non–Neuronal Systems

Biology ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 361
Author(s):  
Myeongwoo Jung ◽  
Eun-Kyung Lee
Keyword(s):  
Gene Expression ◽  
Neural Plasticity ◽  
Molecular Mechanisms ◽  
Neuronal Development ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Novel Treatments ◽  
Target Mrnas ◽  
Neuronal Systems

HuD (also known as ELAVL4) is an RNA–binding protein belonging to the human antigen (Hu) family that regulates stability, translation, splicing, and adenylation of target mRNAs. Unlike ubiquitously distributed HuR, HuD is only expressed in certain types of tissues, mainly in neuronal systems. Numerous studies have shown that HuD plays essential roles in neuronal development, differentiation, neurogenesis, dendritic maturation, neural plasticity, and synaptic transmission by regulating the metabolism of target mRNAs. However, growing evidence suggests that HuD also functions as a pivotal regulator of gene expression in non–neuronal systems and its malfunction is implicated in disease pathogenesis. Comprehensive knowledge of HuD expression, abundance, molecular targets, and regulatory mechanisms will broaden our understanding of its role as a versatile regulator of gene expression, thus enabling novel treatments for diseases with aberrant HuD expression. This review focuses on recent advances investigating the emerging role of HuD, its molecular mechanisms of target gene regulation, and its disease relevance in both neuronal and non–neuronal systems.

scholarly journals Identification and Functional Outcome of mRNAs Associated with RNA-Binding Protein TIA-1

2005 ◽  
Vol 25 (21) ◽  
pp. 9520-9531 ◽  
Author(s):  
Isabel López de Silanes ◽  
Stefanie Galbán ◽  
Jennifer L. Martindale ◽  
Xiaoling Yang ◽  
Krystyna Mazan-Mamczarz ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Cellular Damage ◽  
Necrosis Factor Alpha ◽  
Target Mrnas ◽  
Common Motif ◽  
Tnf Α ◽  
Cox 2 ◽  
Rna Complexes

ABSTRACT The RNA-binding protein TIA-1 (T-cell intracellular antigen 1) functions as a posttranscriptional regulator of gene expression and aggregates to form stress granules following cellular damage. TIA-1 was previously shown to bind mRNAs encoding tumor necrosis factor alpha (TNF-α) and cyclooxygenase 2 (COX-2), but TIA-1 target mRNAs have not been systematically identified. Here, immunoprecipitation (IP) of TIA-1-RNA complexes, followed by microarray-based identification and computational analysis of bound transcripts, was used to elucidate a common motif present among TIA-1 target mRNAs. The predicted TIA-1 motif was a U-rich, 30- to 37-nucleotide (nt)-long bipartite element forming loops of variable size and a bent stem. The TIA-1 motif was found in the TNF-α and COX-2 mRNAs and in 3,019 additional UniGene transcripts (∼3% of the UniGene database), localizing preferentially to the 3′ untranslated region. The interactions between TIA-1 and target transcripts were validated by IP of endogenous mRNAs, followed by reverse transcription and PCR-mediated detection, and by pulldown of biotinylated RNAs, followed by Western blotting. Further studies using RNA interference revealed that TIA-1 repressed the translation of bound mRNAs. In summary, we report a signature motif present in mRNAs that associate with TIA-1 and provide support to the notion that TIA-1 represses the translation of target transcripts.

scholarly journals RNA-binding protein DUS16 plays an essential role in primary miRNA processing in the unicellular alga Chlamydomonas reinhardtii

2016 ◽  
Vol 113 (38) ◽  
pp. 10720-10725 ◽  
Author(s):  
Tomohito Yamasaki ◽  
Masayuki Onishi ◽  
Eun-Jeong Kim ◽  
Heriberto Cerutti ◽  
Takeshi Ohama
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Essential Role ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Mature Mirnas ◽  
Mirna Biogenesis ◽  
Dsrna Binding

Canonical microRNAs (miRNAs) are embedded in duplexed stem–loops in long precursor transcripts and are excised by sequential cleavage by DICER nuclease(s). In this miRNA biogenesis pathway, dsRNA-binding proteins play important roles in animals and plants by assisting DICER. However, these RNA-binding proteins are poorly characterized in unicellular organisms. Here we report that a unique RNA-binding protein, Dull slicer-16 (DUS16), plays an essential role in processing of primary-miRNA (pri-miRNA) transcripts in the unicellular green alga Chlamydomonas reinhardtii. In animals and plants, dsRNA-binding proteins involved in miRNA biogenesis harbor two or three dsRNA-binding domains (dsRBDs), whereas DUS16 contains one dsRBD and also an ssRNA-binding domain (RRM). The null mutant of DUS16 showed a drastic reduction in most miRNA species. Production of these miRNAs was complemented by expression of full-length DUS16, but the expression of RRM- or dsRBD-truncated DUS16 did not restore miRNA production. Furthermore, DUS16 is predominantly localized to the nucleus and associated with nascent (unspliced form) pri-miRNAs and the DICER-LIKE 3 protein. These results suggest that DUS16 recognizes pri-miRNA transcripts cotranscriptionally and promotes their processing into mature miRNAs as a component of a microprocessor complex. We propose that DUS16 is an essential factor for miRNA production in Chlamydomonas and, because DUS16 is functionally similar to the dsRNA-binding proteins involved in miRNA biogenesis in animals and land plants, our report provides insight into this mechanism in unicellular eukaryotes.

scholarly journals Identification of a signature motif in target mRNAs of RNA-binding protein AUF1

2008 ◽  
Vol 37 (1) ◽  
pp. 204-214 ◽  
Author(s):  
Krystyna Mazan-Mamczarz ◽  
Yuki Kuwano ◽  
Ming Zhan ◽  
Elizabeth J. White ◽  
Jennifer L. Martindale ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Target Mrnas ◽  
Signature Motif

scholarly journals RNA-binding protein HuR promotes growth of small intestinal mucosa by activating the Wnt signaling pathway

2014 ◽  
Vol 25 (21) ◽  
pp. 3308-3318 ◽  
Author(s):  
Lan Liu ◽  
Eleni Christodoulou-Vafeiadou ◽  
Jaladanki N. Rao ◽  
Tongtong Zou ◽  
Lan Xiao ◽  
...  
Keyword(s):  
Small Intestine ◽  
Intestinal Epithelium ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Wnt Signaling Pathway ◽  
Small Intestinal Mucosa ◽  
Mucosal Atrophy ◽  
Target Mrnas

Inhibition of growth of the intestinal epithelium, a rapidly self-renewing tissue, is commonly found in various critical disorders. The RNA-binding protein HuR is highly expressed in the gut mucosa and modulates the stability and translation of target mRNAs, but its exact biological function in the intestinal epithelium remains unclear. Here, we investigated the role of HuR in intestinal homeostasis using a genetic model and further defined its target mRNAs. Targeted deletion of HuR in intestinal epithelial cells caused significant mucosal atrophy in the small intestine, as indicated by decreased cell proliferation within the crypts and subsequent shrinkages of crypts and villi. In addition, the HuR-deficient intestinal epithelium also displayed decreased regenerative potential of crypt progenitors after exposure to irradiation. HuR deficiency decreased expression of the Wnt coreceptor LDL receptor–related protein 6 (LRP6) in the mucosal tissues. At the molecular level, HuR was found to bind the Lrp6 mRNA via its 3′-untranslated region and enhanced LRP6 expression by stabilizing Lrp6 mRNA and stimulating its translation. These results indicate that HuR is essential for normal mucosal growth in the small intestine by altering Wnt signals through up-regulation of LRP6 expression and highlight a novel role of HuR deficiency in the pathogenesis of intestinal mucosal atrophy under pathological conditions.

scholarly journals Whi3, an S. cerevisiae RNA-Binding Protein, Is a Component of Stress Granules That Regulates Levels of Its Target mRNAs

PLoS ONE ◽  
2013 ◽  
Vol 8 (12) ◽  
pp. e84060 ◽  
Author(s):  
Kristen J. Holmes ◽  
Daniel M. Klass ◽  
Evan L. Guiney ◽  
Martha S. Cyert
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Stress Granules ◽  
Target Mrnas

scholarly journals The RNA-Binding Protein Rasputin/G3BP Enhances the Stability and Translation of Its Target mRNAs

Cell Reports ◽  
2020 ◽  
Vol 30 (10) ◽  
pp. 3353-3367.e7 ◽  
Author(s):  
John D. Laver ◽  
Jimmy Ly ◽  
Allison K. Winn ◽  
Angelo Karaiskakis ◽  
Sichun Lin ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Target Mrnas ◽  
The Stability

The RNA Binding Protein HuR: a Promising Drug Target for Anticancer Therapy

2019 ◽  
Vol 19 (5) ◽  
pp. 382-399 ◽  
Author(s):  
Mingxia Wu ◽  
Christy W.S. Tong ◽  
Wei Yan ◽  
Kenneth K.W. To ◽  
William C.S. Cho
Keyword(s):  
Targeted Delivery ◽  
High Throughput Screening ◽  
Drug Target ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Target Mrnas ◽  
Recognition Motifs ◽  
The Stability ◽  
And Function

The stability of mRNA is one of the key factors governing the regulation of eukaryotic gene expression and function. Human antigen R (HuR) is an RNA-binding protein that regulates the stability, translation, and nucleus-to-cytoplasm shuttling of its target mRNAs. While HuR is normally localized within the nucleus, it has been shown that HuR binds mRNAs in the nucleus and then escorts the mRNAs to the cytoplasm where HuR protects them from degradation. It contains several RNA recognition motifs, which specifically bind to adenylate and uridylate-rich regions within the 3’-untranslated region of the target mRNA to mediate its effect. Many of the HuR target mRNAs encode proteins important for cell growth, tumorigenesis, angiogenesis, tumor inflammation, invasion and metastasis. HuR overexpression is known to correlate well with high-grade malignancy and poor prognosis in many tumor types. Thus, HuR has emerged as an attractive drug target for cancer therapy. Novel small molecule HuR inhibitors have been identified by high throughput screening and new formulations for targeted delivery of HuR siRNA to tumor cells have been developed with promising anticancer activity. This review summarizes the significant role of HuR in cancer development, progression, and poor treatment response. We will discuss the potential and challenges of targeting HuR therapeutically.

scholarly journals The RNA-binding protein RGGA is a sugar-responsive cofactor of the 5'-3' exonuclease XRN4 that post-transcriptionally meditates plant growth

2021 ◽  
Author(s):  
Hongmei Liu ◽  
Ru Yu ◽  
Hong Zhang ◽  
Xinlei Gao ◽  
Changxiang Zhu ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Critical Role ◽  
Rna Binding Protein ◽  
Growth Potential ◽  
Transcriptional Level ◽  
Interaction Domain ◽  
Target Mrnas ◽  
Sucrose Supply ◽  
Regulated Gene Expression

Abstract Sugar-regulated gene expression is a ubiquitous mechanism for carbohydrate allocation and utilization by keeping a balance among source and sink organs in plants. Previous studies have shown that excess sugar represses the expression of the genes implicated in photosynthesis and sugar metabolism. However, the mechanism is still largely unknown. Here, we found that the mutant of Arabidopsis RGGA, RGG repeats RNA-binding protein A coding gene, grew faster than wild type (Col-0) in MS medium. In rgga, mRNA half-live of the genes related to sucrose transport and metabolism, chlorophyll synthesis, root development as well as certain transcription factors was obviously longer than those of Col-0. Further study revealed that AtRGGA could interact with 5'-3' exonuclease AtXRN4, and guide it to the target mRNAs for their degradation. When AtRGGA is absent or its interaction domain is deleted, AtXRN4 self can't recognize the target mRNAs, which leads to a dramatically increase in transcript levels of the above gene subsets, and thus promotes the growth of Arabidopsis with exogenous sucrose supply. And only 5-day sucrose supply could trigger the vigorous growth of rgga. These findings suggest that the regulation of mRNA stability mediated by RGGA plays a critical role in sugar suppression, and implicates a possibility to unlock the growth potential by modulating sugar utilization at post-transcriptional level in plants.

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