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Non-VLPs
Published in Paul Pumpens, Single-Stranded RNA Phages, 2020
The MS2-based tethering allowed functional identification of the following important protein players: Y14, a component of the exon junction complex, which underwent post-translational modifications (Hsu et al. 2005, Chuang et al. 2013); the Xenopus laevis and human DAZ-associated protein 1 (DAZAP1), an RNA-binding protein required for normal growth, development, and fertility (Smith et al. 2011); Ki-1/57 protein from Hodgkin lymphoma (de Almeida Gonçalves et al. 2011); a quadruple BEN domain-containing protein (BEND3) that was highly conserved among vertebrates (Sathyan et al. 2011); Staufen 1 (Kim et al. 2005; Cho et al. 2013a) and Staufen2 (Miki et al. 2011), double-stranded RNA-binding proteins and mammalian orthologs of the Staufen protein in Drosophila melanogaster, the DEAD-Box Protein Dhh1 in yeast (Sweat et al. 2012); Ewing sarcoma protein (Huang L et al. 2012); AUF1, an AU-rich element binding factor heterogeneous nuclear ribonucleoprotein D (1/hnRNP D), as an interacting protein of Epstein-Barr virus−induced noncoding RNA EBER1 (Lee N et al. 2012); and PARP12, a member of a large family of ADP-ribosyl transferases, encoded by an interferon-induced gene (Welsby et al. 2014).
Transport of mRNA into the Cytoplasm
Published in Alvaro Macieira-Coelho, Molecular Basis of Aging, 2017
Werner E. G. Müller, Paul S. Agutter, Heinz C. Schröder
In addition, AU-rich elements occurring in the 3′-terminal nontranslated region of some cytokine- (e.g., tumor-necrosis factor, interleukin) and oncogene-mRNAs (e.g., fos, myc, and sis) may serve as recognition sequences for binding proteins. We demonstrated that the AU-specific endoribonuclease V47 degrades AU-rich mRNA in unstimulated macrophages.48 This degradation is prevented by a cytosolic protein (adenosine-uridine binding factor, AU binding protein49,50), which binds to the AUUUA motif of these mRNAs and thereby prolongs their half lives.51 We could show that this protein is also able to selectively increase transport of AU-rich RNAs after binding to AUUUA. A hypothetical scheme of the mode of action of AU binding protein is shown in Figure 4.
Human Herpesvirus Type 8/Kaposi Sarcoma Herpesvirus
Published in Satya Prakash Gupta, Cancer-Causing Viruses and Their Inhibitors, 2014
Hiba El Hajj, Raghida Abou Merhi, Ali Bazarbachi
Along with the proteins of the latency locus, kaposin (also known as K12) is expressed in most HHV-8-infected spindle tumor cells (Kliche et al. 2001). The most common mRNA transcript encoded by the K12 locus is actually 1.5–2.3 kb in size (Kliche et al. 2001), and the translation program for K12 is complex, using canonical and alternative translation initiation codons to encode three proteins (kaposin A, kaposin B, and kaposin C) (Sadler et al. 1999). Although functional characterization of kaposin A and B has been investigated and carried out, no function has been ascribed to kaposin C to date. Kaposin A is a highly hydrophobic type II transmembrane protein and is expressed on the cell surface (Kliche et al. 2001). Kaposin A might activate the extracellular signal regulated kinase (ERK)-1/2 MAPK activated protein Kinase 2 pathway (Table 10.2) and downstream AP-1235 through its interaction with cytohesin-1, a guanine nucleotide exchange factor that regulates the function of β-integrins (Muralidhar et al. 2000). Kaposin B is a 38 kDa protein (Tomkowicz et al. 2002) that upregulates cytokine expression by blocking the degradation of their mRNA transcripts and binds to and activates mitogen activated protein kinase (MK2) resulting in the inhibition of adenylate-uridylate (AU)-rich elements (AREs)-mediated mRNA degradation (McCormick and Ganem 2005).
First Report of the 3'-Untranslated Region +1506 (A>C) [NM_000518.5: c.*32A>C] mutation on the β-Globin Gene in the Indian Population
Published in Hemoglobin, 2021
Aditi Sen, Venu Seenappa, Prantar Chakrabarti, Tuphan Kanti Dolai
The adenylate uridylate (AU-rich) elements (AREs) are the most common regulatory elements in the 3′-UTR responsible for mRNA (de)stabilization and alternative pre-mRNA processing. A basic motif in AREs is represented by the pentamer ‘AUUUA’ that occurs in variable-length repetitions in the regions rich for uracil and interspersed with adenine. Usually, they encompass the facilitation of the deadenylation process resulting in the accelerated shortening of polyadenylation (polyA) tail, which is crucial for mRNA stability [5]. Therefore, a mutation in this region might be involved in the reduction of β-globin chain production. Here, we report a very rare mutation located in the first AU motif of 3′-UTR of the β-globin gene for the first time in India during mutation screening for prenatal diagnosis (PND) of an at-risk couple, and attempt to elucidate the resulting phenotype.
New insights into the novel anti-inflammatory mode of action of glucocorticoids
Published in Immunopharmacology and Immunotoxicology, 2020
Deepa K. Ingawale, Satish K. Mandlik
The variety of pro-inflammatory cytokine mRNAs is destabilizes by zinc finger protein TTP by binding to AU-rich elements (ARE) subjecting them for degradation. It is a protein that destabilizes the mRNA that identifies specific transcripts and produces degradation by exonucleases enzymes [166]. A TTP knockout inflammatory arthritic mouse model is characterized by elevated stability of TNF mRNA and augmented TNF protein expression [167]. Colony stimulating factor-2 (CSF2), Cyclo-oxygenaase-2 (COX-2) and Interleukin-2 (IL-2) genes are dysregulated in the deficiency of TTP and the expressions of further inflammatory mediators will be controlled by TTP [168]. The stabilization of inflammatory mRNAs can be done by phosphorylation and inactivation of TTP by MAPK-activated protein kinase 2 [169]. The dexamethasone activity on various cells such as pulmonary epithelial cells (A549 and BEAS-2B), human keratinocytes [170] or HeLa cells elevates the expression of TTP mRNA. Diminution of TTP expression by siRNA decreases the inhibitory effect of dexamethasone on endogenous TNF mRNA expression. Hence, stimulation of TTP gene may responsible for the post-transcriptional inhibitory effects of GCs that would leads to the development of novel anti-inflammatory approaches to battle against inflammatory disease.
RNA binding proteins in the control of autoimmune diseases
Published in Immunological Medicine, 2019
Masanori Yoshinaga, Osamu Takeuchi
Cis-elements are composed of two factors, primary sequences and secondary structures. On the one hand, a well-known immune-related cis-element, the AU-rich element (ARE) is defined by primary sequences. AREs are sequences rich in A and U nucleotides, typically containing a repetition of AUUUA pentamers. While AREs are defined mainly by its primary sequence, the secondary structures formed within AREs may also regulate the binding of ARE-binding proteins [20,21]. On the other hand, another immune-related cis-element, the stem-loop element is defined by a combination of both of the above-mentioned factors. Stem-loop elements are hairpin-like structures. Besides its secondary structure, loop sequences are also important for the recognition by RBPs (Figure 3) [22]. This dual dependency is a characteristic shared with other cis-elements such as iron regulatory elements (IRE), histone 3′ UTR elements and selenocysteine insertion sequences (SECIS) [23–25]. While these canonical sequences are core requirements, it is often unclear whether there are additional constraints for determining the binding affinity with RBPs.