ICP27 interacts with the RNA export factor Aly/REF to direct herpes simplex virus type 1 intronless mRNAs to the TAP export pathway.
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Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through Nup62, inhibiting host nucleocytoplasmic transport pathwaysNuclear relocalisation of cytoplasmic poly(A)-binding proteins PABP1 and PABP4 in response to UV irradiation reveals mRNA-dependent export of metazoan PABPsAPOBEC1-mediated editing and attenuation of herpes simplex virus 1 DNA indicate that neurons have an antiviral role during herpes simplex encephalitisRNA-binding of the human cytomegalovirus transactivator protein UL69, mediated by arginine-rich motifs, is not required for nuclear export of unspliced RNA.Structural Basis for the Recognition of Cellular mRNA Export Factor REF by Herpes Viral Proteins HSV-1 ICP27 and HVS ORF57Competitive and Cooperative Interactions Mediate RNA Transfer from Herpesvirus Saimiri ORF57 to the Mammalian Export Adaptor ALYREFIdentification of herpes simplex virus RNAs that interact specifically with regulatory protein ICP27 in vivo.Hsc70 focus formation at the periphery of HSV-1 transcription sites requires ICP27.ICP27 phosphorylation site mutants are defective in herpes simplex virus 1 replication and gene expression.ICP27 phosphorylation site mutants display altered functional interactions with cellular export factors Aly/REF and TAP/NXF1 but are able to bind herpes simplex virus 1 RNARegulation of viral gene expression by duck enteritis virus UL54.ICP27 recruits Aly/REF but not TAP/NXF1 to herpes simplex virus type 1 transcription sites although TAP/NXF1 is required for ICP27 export.Control of VP16 translation by the herpes simplex virus type 1 immediate-early protein ICP27.Herpes simplex virus 1 regulatory protein ICP27 undergoes a head-to-tail intramolecular interaction.Herpes simplex virus ICP27 activation of stress kinases JNK and p38.Binding of hnRNP L to the pre-mRNA processing enhancer of the herpes simplex virus thymidine kinase gene enhances both polyadenylation and nucleocytoplasmic export of intronless mRNAs.Three arginine residues within the RGG box are crucial for ICP27 binding to herpes simplex virus 1 GC-rich sequences and for efficient viral RNA export.Head-to-tail intramolecular interaction of herpes simplex virus type 1 regulatory protein ICP27 is important for its interaction with cellular mRNA export receptor TAP/NXF1.Direct stimulation of translation by the multifunctional herpesvirus ICP27 protein.Export of adenoviral late mRNA from the nucleus requires the Nxf1/Tap export receptor.ICP27 interacts with the C-terminal domain of RNA polymerase II and facilitates its recruitment to herpes simplex virus 1 transcription sites, where it undergoes proteasomal degradation during infection.ICP27 selectively regulates the cytoplasmic localization of a subset of viral transcripts in herpes simplex virus type 1-infected cellsKaposi's sarcoma-associated herpesvirus lytic gene ORF57 is essential for infectious virion productionInhibition of cdk9 during herpes simplex virus 1 infection impedes viral transcriptionImaging of mRNA-protein interactions in live cells using novel mCherry trimolecular fluorescence complementation systemsArginine methylation of the RGG box does not appear to regulate ICP27 import during herpes simplex virus infection.Herpes simplex virus ICP27 is required for virus-induced stabilization of the ARE-containing IEX-1 mRNA encoded by the human IER3 geneKSHV ORF57, a protein of many facesExport and stability of naturally intronless mRNAs require specific coding region sequences and the TREX mRNA export complexSelective recruitment of nuclear factors to productively replicating herpes simplex virus genomes.Multiple roles of Epstein-Barr virus SM protein in lytic replication.Structure of the C-Terminal Domain of the Multifunctional ICP27 Protein from Herpes Simplex Virus 1Kaposi's sarcoma-associated herpesvirus ORF57 protein enhances mRNA accumulation independently of effects on nuclear RNA export.Binding of cellular export factor REF/Aly by Kaposi's sarcoma-associated herpesvirus (KSHV) ORF57 protein is not required for efficient KSHV lytic replication.The structure of the folded domain from the signature multifunctional protein ICP27 from herpes simplex virus-1 reveals an intertwined dimer.Kaposi's sarcoma-associated herpesvirus ORF57 is not a bona fide export factor.Distribution and dynamics of transcription-associated proteins during parvovirus infection.Kaposi's sarcoma-associated herpesvirus ORF57 functions as a viral splicing factor and promotes expression of intron-containing viral lytic genes in spliceosome-mediated RNA splicing.Herpes simplex virus ICP27 increases translation of a subset of viral late mRNAs.mRNA decay during herpes simplex virus (HSV) infections: mutations that affect translation of an mRNA influence the sites at which it is cleaved by the HSV virion host shutoff (Vhs) protein.
P2860
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P2860
ICP27 interacts with the RNA export factor Aly/REF to direct herpes simplex virus type 1 intronless mRNAs to the TAP export pathway.
description
2002 nî lūn-bûn
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2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
ICP27 interacts with the RNA e ...... RNAs to the TAP export pathway
@nl
ICP27 interacts with the RNA e ...... NAs to the TAP export pathway.
@ast
ICP27 interacts with the RNA e ...... NAs to the TAP export pathway.
@en
type
label
ICP27 interacts with the RNA e ...... RNAs to the TAP export pathway
@nl
ICP27 interacts with the RNA e ...... NAs to the TAP export pathway.
@ast
ICP27 interacts with the RNA e ...... NAs to the TAP export pathway.
@en
prefLabel
ICP27 interacts with the RNA e ...... RNAs to the TAP export pathway
@nl
ICP27 interacts with the RNA e ...... NAs to the TAP export pathway.
@ast
ICP27 interacts with the RNA e ...... NAs to the TAP export pathway.
@en
P2860
P1433
P1476
ICP27 interacts with the RNA e ...... NAs to the TAP export pathway.
@en
P2093
I-Hsiung Brandon Chen
Kathryn S Sciabica
P2860
P304
12877-12889
P356
10.1128/JVI.76.24.12877-12889.2002
P407
P577
2002-12-01T00:00:00Z