scholarly journals Drosophila Decapping Protein 1, dDcp1, Is a Component of the oskar mRNP Complex and Directs Its Posterior Localization in the Oocyte

2006 ◽  
Vol 10 (5) ◽  
pp. 601-613 ◽  
Author(s):  
Ming-Der Lin ◽  
Shih-Jung Fan ◽  
Wei-Shan Hsu ◽  
Tze-Bin Chou
Keyword(s):  
Mrnp Complex

scholarly journals Human Immunodeficiency Virus Type 1 Vif Protein Is an Integral Component of an mRNP Complex of Viral RNA and Could Be Involved in the Viral RNA Folding and Packaging Process

2000 ◽  
Vol 74 (18) ◽  
pp. 8252-8261 ◽  
Author(s):  
Hui Zhang ◽  
Roger J. Pomerantz ◽  
Geethanjali Dornadula ◽  
Yong Sun
Keyword(s):  
Human Immunodeficiency Virus ◽  
Rna Binding ◽  
Viral Rna ◽  
Immunodeficiency Virus ◽  
Mrnp Complex ◽  
Rna Interaction ◽  
Vif Protein ◽  
Hiv 1

ABSTRACT Virion infectivity factor (Vif) is a protein encoded by human immunodeficiency virus types 1 and 2 (HIV-1 and -2) and simian immunodeficiency virus, plus other lentiviruses, and is essential for viral replication either in vivo or in culture for nonpermissive cells such as peripheral blood lymphoid cells, macrophages, and H9 T cells. Defects in the vif gene affect virion morphology and reverse transcription but not the expression of viral components. It has been shown that Vif colocalizes with Gag in cells and Vif binds to the NCp7 domain of Gag in vitro. However, it seems that Vif is not specifically packaged into virions. The molecular mechanism(s) for Vif remains unknown. In this report, we demonstrate that HIV-1 Vif is an RNA-binding protein and specifically binds to HIV-1 genomic RNA in vitro. Further, Vif binds to HIV-1 RNA in the cytoplasm of virus-producing cells to form a 40S mRNP complex. Coimmunoprecipitation and in vivo UV cross-linking assays indicated that Vif directly interact with HIV-1 RNA in the virus-producing cells. Vif-RNA binding could be displaced by Gag-RNA binding, suggesting that Vif protein in the mRNP complex may mediate viral RNA interaction with HIV-1 Gag precursors. Furthermore, we have demonstrated that these Vif mutants that lose the RNA binding activity in vitro do not supportvif-deficient HIV-1 replication in H9 T cells, suggesting that the RNA binding capacity of Vif is important for its function. Further studies regarding Vif-RNA interaction in virus-producing cells will be important for studying the function of Vif in the HIV-1 life cycle.

scholarly journals Structural and Functional Analysis of an mRNP Complex That Mediates the High Stability of Human β-Globin mRNA

2001 ◽  
Vol 21 (17) ◽  
pp. 5879-5888 ◽  
Author(s):  
Jia Yu ◽  
J. Eric Russell
Keyword(s):  
Mrna Stability ◽  
Rna Binding ◽  
Assembly Sequence ◽  
Regulatory Pathway ◽  
Globin Mrna ◽  
Mrnp Complex ◽  
The Stability ◽  
High Level

ABSTRACT Human globins are encoded by mRNAs exhibiting high stabilities in transcriptionally silenced erythrocyte progenitors. Unlike α-globin mRNA, whose stability is enhanced by assembly of a specific messenger RNP (mRNP) α complex on its 3′ untranslated region (UTR), neither the structure(s) nor the mechanism(s) that effects the high-level stability of human β-globin mRNA has been identified. The present work describes an mRNP complex assembling on the 3′ UTR of the β-globin mRNA that exhibits many of the properties of the stability-enhancing α complex. The β-globin mRNP complex is shown to contain one or more factors homologous to αCP, a 39-kDa RNA-binding protein that is integral to α-complex assembly. Sequence analysis implicates a specific 14-nucleotide pyrimidine-rich track within its 3′ UTR as the site of β-globin mRNP assembly. The importance of this track to mRNA stability is subsequently verified in vivo using mice expressing human β-globin transgenes that contain informative mutations in this region. In combination, the in vitro and in vivo analyses indicate that the high stabilities of the α- and β-globin mRNAs are maintained through related mRNP complexes that may share a common regulatory pathway.

scholarly journals Unveiling the partners of the DRBD2-mRNP complex, an RBP in Trypanosoma cruzi and ortholog to the yeast SR-protein Gbp2

2019 ◽  
Vol 19 (1) ◽  
Author(s):  
Helisa Helena Wippel ◽  
Juliane Soldi Malgarin ◽  
Alexandre Haruo Inoue ◽  
Felipe da Veiga Leprevost ◽  
Paulo Costa Carvalho ◽  
...  
Keyword(s):  
Trypanosoma Cruzi ◽  
Sr Protein ◽  
Mrnp Complex

scholarly journals A feedback loop between Wolbachia and the Drosophila gurken mRNP complex influences Wolbachia titer

2011 ◽  
Vol 124 (24) ◽  
pp. 4299-4308 ◽  
Author(s):  
Laura R. Serbus ◽  
Amy Ferreccio ◽  
Mariya Zhukova ◽  
Chanel L. McMorris ◽  
Elena Kiseleva ◽  
...  
Keyword(s):  
Feedback Loop ◽  
Mrnp Complex

scholarly journals Identification of an mRNP Complex Regulating Tumorigenesis at the Translational Elongation Step

2011 ◽  
Vol 41 (4) ◽  
pp. 419-431 ◽  
Author(s):  
George S. Hussey ◽  
Arindam Chaudhury ◽  
Andrea E. Dawson ◽  
Daniel J. Lindner ◽  
Charlotte R. Knudsen ◽  
...  
Keyword(s):  
Mrnp Complex ◽  
Elongation Step

scholarly journals Neurotrophin-Induced Transport of a β-Actin mRNP Complex Increases β-Actin Levels and Stimulates Growth Cone Motility

Neuron ◽  
2001 ◽  
Vol 31 (2) ◽  
pp. 261-275 ◽  
Author(s):  
H.L. Zhang ◽  
T. Eom ◽  
Y. Oleynikov ◽  
S.M. Shenoy ◽  
D.A. Liebelt ◽  
...  
Keyword(s):  
Growth Cone ◽  
Mrnp Complex

scholarly journals Assessing the partners of the RBP9-mRNP complex in Trypanosoma cruzi using shotgun proteomics and RNA-seq

RNA Biology ◽  
2018 ◽  
pp. 1-13 ◽  
Author(s):  
Helisa Helena Wippel ◽  
Alexandre Haruo Inoue ◽  
Newton Medeiros Vidal ◽  
Jimena Ferreira da Costa ◽  
Bruna Hilzendeger Marcon ◽  
...  
Keyword(s):  
Trypanosoma Cruzi ◽  
Shotgun Proteomics ◽  
Rna Seq ◽  
Mrnp Complex
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