rev protein of human immunodeficiency virus type 1 affects the stability and transport of the viral mRNA.

Felber, Barbara K.; Hadzopoulou-Cladaras, Margarita; Cladaras, Christos; Copeland, Terry D.; Pavlakis, George N.

doi:10.1073/pnas.86.5.1495

Cited by 584 publications

(617 citation statements)

References 22 publications

(25 reference statements)

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“…This is consistent with our earlier results which demonstrated that the human immunode®ency type 1 (HIV-1) Rev/RRE regulatory axis could overcome the inhibitory e ect of the h1ARE . The HIV-1 Rev protein binds to its target RNA element in the nucleus and acts by promoting export of nuclear mRNAs (Emerman et al, 1989;Felber et al, 1989;HammarskjoÈ ld et al, 1989;Malim et al, 1989) through an alternative, productive route (Bogerd et al, 1995;Fisher et al, 1995;Fritz et al, 1995), thereby presumably preventing the h1ARE from interacting with nuclear proteins that mediate inhibition as the mRNA enters the cytoplasm. Recent reports have described the identi®cation of an RNaseE like activity in mammalian cells and have shown that partially puri®ed mammalian RNaseE cleaves AUUUA containing RNAs in vitro (Wennborg et al, 1995).…”

Section: Discussionmentioning

confidence: 99%

AU-rich mRNA instability elements on human papillomavirus type 1 late mRNAs and c-fos mRNAs interact with the same cellular factors

et al. 1997

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Expression levels of human papillomavirus type 1 late genes are determined in part by an AU-rich inhibitory sequence in the 3' untranslated region on the late mRNAs. Fine mapping of the AU rich inhibitory sequence revealed that it mapped to a 57 nucleotide sequence, consisting of an AU-rich region containing two AUUUA motifs and a U-rich region containing three UUUUU motifs. An internal deletion showed that the Urich region was required for inhibition. Point mutations in the AUUUA-and UUUUU-motifs inactivated the inhibitory sequence. Analysis of the stability of mRNAs containing the AU-rich sequence in sense or anti-sense orientation showed that mRNAs containing the AU-rich sequence in sense orientation had reduced half life. Analysis of RNA-protein interactions revealed that binding to the inhibitory sequence of three poly(U) binding proteins (38, 44 and 46 kDa) correlated with inhibition and that the same proteins bind to the AU-rich mRNA instability element in the 3' untranslated region on the human c-fos mRNA. We speculate that the human papillomavirus late mRNAs, produced from several hundred copies of the virus genome present in infected cells, compete with the c-fos mRNAs for destabilizing cellular factors and that this may lead to elevated Fos protein levels in human papillomavirus infected cells

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Section: Discussionmentioning

confidence: 99%

AU-rich mRNA instability elements on human papillomavirus type 1 late mRNAs and c-fos mRNAs interact with the same cellular factors

et al. 1997

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“…The major discrepancy concerns the presenee of PAB II in the nucleolus, in wh ich poly(A) has not been found [30]. Other nuclear RNA bin ding proteins involved in mRN A metabolism have been detected in the nucleolus as weil, even though no nucleolar hmction of these proteins is known [31,32]. Nonspecific binding of an abundant protein to ribosomal RNA (see above) might be an explanation.…”

Section: Resul Ts and Discussionmentioning

confidence: 99%

Immunodetection of Poly(A) Binding Protein II in the Cell Nucleus

Krause

Fakan

Weis

et al. 1994

Experimental Cell Research

116

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During the polyadenylation of pre-mRN A in vitro~ poly(A) binding protein 11 (PAB 11) bind. to tbe growing poly(A) taH, stimulating its extension. Tbe subcellular localization of PAß 11 was investigated witb an antibody affinity-purified from rabbit serum raised against the purified protein. Immunoßuorescence microscopy detected PAß 11 exclusively in tbe cell nueleus, botb in a widespread staining and in more intensely stained "speckles." PAß 11 was excluded from the nucleoli. ßy electron microscopy, PAß II was also found almost exclusively in the nucleus, predominantly in clusters of interchromatin granules, likely corresponding to the speckles observed by immunofluorescence microscopy, and in perichromatin fibrils, wbich represent nascent transeripts and probably tbe sites of pre-mRN A processing. In addition, electron microscopy also detected P AB 11 in nucleoli. Tbe distribution corresponds largely to that of other factors involved in the processing of premRNA and is thus in agreement witb the proposed role of the protein in polyadenylation.

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“…26 Rev also increases RNA stability and translation. 27 In contrast, the constitutive transport element (CTE) of Mason-Pfizer monkey virus mediates the export of unspliced RNA through the cellular RNA export factor Tap. 28 We hypothesized that the export of partially doublestranded genomic bidirectional vector RNA depends on Rev's function to overcome nuclear quality control restrictions.…”

Section: Introductionmentioning

confidence: 99%

Mechanisms controlling titer and expression of bidirectional lentiviral and gammaretroviral vectors

et al. 2009

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Bidirectional lentiviral vectors mediate expression of two or more cDNAs from a single internal promoter. In this study, we examined mechanisms that control titer and expression properties of this vector system. To address whether the bidirectional design depends on lentiviral (LV) backbone components, especially the Rev/Rev responsive element (RRE) system, we constructed similar expression cassettes for LV and gammaretroviral (GV) vectors. Bidirectional expression levels could be adjusted by the use of different internal promoters. Furthermore, removal of the constitutive RNA transport element of Mason-Pfizer monkey virus, used in first generation bidirectional LV vectors, improved gene expression. Titers of bidirectional vectors were B10-fold reduced in comparison to unidirectional vectors, independent of the Rev/RRE interaction. We reasoned that titer reductions were due to the formation of interfering double-stranded RNA in packaging cells. Indeed, cotransfection of Nodamuravirus B2 protein, an RNA interference suppressor, increased bidirectional vector titers at least fivefold. We validated the potential of high titer bidirectional vectors by coexpressing a fluorescent marker with O 6 -methylguanine-DNA methyltransferase from integrating, or with Cre recombinase from integrating and non-integrating GV and LV backbones. This allowed for the tracking of chemoprotected and recombined cells by fluorescence marker expression.

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rev protein of human immunodeficiency virus type 1 affects the stability and transport of the viral mRNA.

Cited by 584 publications

References 22 publications

AU-rich mRNA instability elements on human papillomavirus type 1 late mRNAs and c-fos mRNAs interact with the same cellular factors

AU-rich mRNA instability elements on human papillomavirus type 1 late mRNAs and c-fos mRNAs interact with the same cellular factors

Immunodetection of Poly(A) Binding Protein II in the Cell Nucleus

Mechanisms controlling titer and expression of bidirectional lentiviral and gammaretroviral vectors

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