RNA-protein interactions within the 3"untranslated region (3"UTR) of the human multidrug resistance type 1 (MDR1)

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  • English
National Library of Canada , Ottawa
SeriesCanadian theses = -- Thèses canadiennes
The Physical Object
Pagination2 microfiches : negative. --
ID Numbers
Open LibraryOL20800017M
ISBN 100612541606

Introduction. The importance of the mRNA 3′ untranslated region (3′UTR) as a repository for signals determining mRNA processing, polyadenylation, export, stability, localization, translation and cell cycle regulation has become apparent ().A summary of this work indicates that critical RNA-protein interactions are involved and a multitude of RNA elements and binding proteins are being Cited by:   Several functions have been attributed to protein binding within the 3'untranslated region (3'UTR) of mRNA, including mRNA localization, stability, and translational repression.

Vimentin is an intermediate filament protein whose 3'untranslated sequence is highly conserved between by: Zendra E. Zehner 0 Rebecca K.

Shepherd 0 Joanna Gabryszuk 0 Tzu-Fun Fu 0 May Al-Ali 0 W. Michael Holmes 0 0 and The Massey Cancer Center, Medical College of Virginia, Virginia Commonwealth University, Richmond Several functions have been attributed to protein binding within the 3 untranslated region (3UTR) of mRNA, including mRNA localization, stability, and translational Cited by: RNA–protein interactions within the 3 ′ untranslated region of vimentin mRNA Zendra E.

Zehner *, Rebecca K. Shepher d, Joanna Gabr yszuk 1, Tzu-Fun Fu. RNA-protein interactions within the 3 ' untranslated region of vimentin mRNA. Z E Zehner Department of Biochemistry and Molecular Biophysics, BoxMedical College of Virginia, Virginia Commonwealth University, Richmond, VAby: – Nucleic Acids Research,Vol.

25, No. 16 Oxford University Press RNA–protein interactions within the 3′ untranslated. In this work, we characterized the RNA-protein interactions within the MDR1 3'UTR to identify regulatory sequences that confer MDR1 mRNA stabilization.

RNA gel shift assays indicated that nt in the MDR1 3' UTR (termed MDRB) was the major protein binding site. RNA-protein interactions within the 3 ' untranslated region of vimentin mRNA.

By Z E Zehner, R K Shepherd, J Gabryszuk, T F Fu, M Al-Ali and W M Holmes. Abstract. Several functions have been attributed to protein binding within the 3'untranslated region (3'UTR) of mRNA, including mRNA localization, stability, and translational repression. The rate of mRNA decay is regulated by the interaction of cis‐acting elements in the transcripts and sequence‐specific RNA‐binding proteins.

One of the most studied cis ‐acting elements is the AU‐rich element (ARE) present in the 3′ untranslated region (3′UTR) of several unstable mRNAs. Collagen α1 (I) mRNA has in the 3′ untranslated region (UTR) a C‐rich sequence that binds protein αCP, this binding stabilizes the mRNA in collagen producing cells.

In the 5′ UTR both collagen mRNAs have a conserved stem‐loop (5′ SL) structure. Kong J, Liebhaber SA () A cell type-restricted mRNA surveillance pathway triggered by ribosome extension into the 3’ untranslated region.

Nat Struct Mol Biol 14(7)– doi/nsmb PubMed CrossRef Google Scholar. It is the site of multiple RNA-protein and RNA-RNA interactions and it plays a critical role during translation initiation. Similar to the 5’UTR, CVB3 3’ untranslated region (3’UTR) also contains secondary structural elements consisting of three stem-loops followed by a poly (A) tail sequence.

We amplified a nucleotide fragment of the transcribed 3′ untranslated region of the TBXA2R gene using the polymerase chain reaction (PCR) and the published cDNA sequence. This region was found to contain two sequence polymorphisms within an Alu.

These DNA polymorphisms were demonstrated using an efficient method of direct solid-phase. Non-radioactive RNA end-labeling techniques are limited, but more versatile biotin and fluorescent labeling methods are now available.

For example, The Thermo Scientific LightShift Chemiluminescent RNA EMSA Kit provides a non-radioactive solution for studying RNA–protein interactions using EMSA.

The 3'-untranslated region length and AU-rich RNA location modulate RNA-protein interaction and translational control of β2-adrenergic receptor mRNA Posttranscriptional controls play a major role in β(2)-adrenergic receptor (β(2)-AR) expression.

Posttranscriptional controls, mediated primarily by RNA-protein complexes, have the potential to alter multiple steps in RNA processing and function. Human alpha-globin mRNA is bound at a C-rich motif in the 3' untranslated region (3'UTR) by the KH domain.

The 3′ untranslated region (UTR) of the hepatitis C virus (HCV) is believed to function in the initiation and regulation of viral RNA replication and protein translation by interacting with the viral and host components.

Translational repression of hunchback (hb) mRNA in the posterior of the Drosophila embryo requires two copies of a bipartite sequence, the Nanos Response Element (NRE), located in the 3‘ untranslated region of the mRNA.

The PUMILIO (PUM) protein is thought to bind the NREs and thereby repress hb translation. The RNA-binding domain of PUM defines an evolutionarily conserved family of RNA. Several regions of the mRNA molecule are not translated into a protein including the 5' cap, 5' untranslated region, 3′ untranslated region and poly (A) tail.

Regulatory regions within the 3′-untranslated region can influence polyadenylation, translation efficiency, localization, and.

Abstract. Numerous recent studies have reported the identification of regulatory sequences located within either the 5′ or 3′ untranslated regions (UTRs) in individual mRNAs which are known to be controlled at the translational level (for review, see ref.

1).It is generally presumed in these cases that the observed mRNA-specific translational regulation is mediated by protein(s. Flanking the coding region are the 5′- and 3′-untranslated regions (UTRs). The 5′-UTR of flaviviruses is relatively short (95– bases in length), while the 3′-UTR is usually longer but demonstrates extensive heterogeneity in size and sequence between different viral species and even among different strains within the same species.

Details RNA-protein interactions within the 3"untranslated region (3"UTR) of the human multidrug resistance type 1 (MDR1) FB2

Interaction of two members of the heterogeneous nuclear ribonucleoprotein (hnRNP) family with the 3′untranslated region (UTR) of the murine inducible nitric-oxide synthase (iNOS) mRNA is demonstrated in this study. An iNOS RNA-protein complex is formed using protein extracts from untreated and septic shock treated mouse liver.

UV cross-linking reveals that the complex consists of. Thus, RNA–protein interactions are crucial for maintaining proper RNA metabolism. To date, sequences that are required for mRNA localization have been found within the 3′UTR of their respective mRNAs.

Such sequences have been termed zipcodes, since they function to direct mRNAs to their final cellular destination (9). Iron-responsive elements (IREs) are RNA motifs that have been identified within the 5' untranslated region of ferritin messenger RNA and the 3' untranslated region of transferrin receptor mRNA.

Download RNA-protein interactions within the 3"untranslated region (3"UTR) of the human multidrug resistance type 1 (MDR1) PDF

A single IRE mediates iron-dependent control of ferritin translation, whereas multiple IREs are found in the region of the transferrin receptor mRNA responsible for iron-dependent control of mRNA stability.

The 90/kDa and kDa species were specifically competed by excess hypoxia stability region RNA. Thus, increased VPF/VEGF mRNA stability induced by hypoxia is mediated, at least in part, by specific interactions between a defined mRNA stability sequence in the 3′ untranslated region and distinct mRNA-binding proteins in human tumor cells.

The non-structural protein NS1 of influenza A viruses is an RNA-binding protein of which its activities in the infected cell contribute to the success of the viral cycle, notably through interferon antagonism.

We have previously shown that NS1 strongly binds RNA aptamers harbouring virus-specific sequence motifs (Marc et al., Nucleic Acids Res.

Description RNA-protein interactions within the 3"untranslated region (3"UTR) of the human multidrug resistance type 1 (MDR1) FB2

41, –). The region of the mRNA between the termination codon and the poly (A) tail — the 3’ untranslated region (3’UTR) — often governs when, where and how much protein an mRNA produces. A key first step in figuring out how 3’UTRs work is identifying the regulators they bind to.

Here, we describe a robust method for RNA electrophoretic mobility shift and UV cross-linking assays that allows rapid detection of cytoplasmic RNA-protein interactions. For added convenience to new investigators, these assays use mini-gels with an electrophoresis time of 15–20 min, enabling a high throughput of samples.

The N-terminal RNP domain of U1A binds two different RNA substrates with high affinity and specificity: stem−loop II of the U1 snRNA and a complex secondary structure in the 3‘-untranslated region (3‘-UTR) of the U1A pre-mRNA. Both RNAs contain a single-stranded sequence which is the main site of interaction with the protein, but in completely different structural contexts.

Here we. Fragile X syndrome, the most common cause of inherited intellectual disability, is caused by a trinucleotide CGG expansion in the 5′-untranslated region of the FMR1 gene, which leads to the loss of expression of the fragile X mental retardation protein (FMRP).

FMRP, an RNA-binding protein that regulates the translation of specific mRNAs, has been shown to bind a subset of its mRNA targets by. tenotomy is an unloading model of muscle atrophy that results in rapid decrease of muscle cell size and protein content ().Tenotomy results in a 34% decrease in wet weight after 1 wk (), and, specifically, decreases the β-myosin heavy chain (β-MHC) protein content of postural muscles such as the soleus ().It is well known that chronic adaptation is mediated by changes at the level of.Amyloidogenic cells overexpress amyloid precursor protein (APP) mRNAs suggesting a transcriptional or post-transcriptional defect may contribute to this process.

We have previously shown that APP mRNAs display regulated stability which is dependent on a base element within the 3'-untranslated region (UTR).cific sequences within the GLUT1 mRNA untranslated re-gion (UTR) (8).

These findings are consistent with other studies showing that cytosolic transacting factors bind specifi-cally to cis-regulatory elements within either the or the UTR of mRNAs to regulate mRNA stability and/or transla-tional efficiency (9–11).