The<i>Herpesvirus saimiri</i>Small Nuclear RNAs Recruit AU-Rich Element-Binding Proteins but Do Not Alter Host AU-Rich Element-Containing mRNA Levels in Virally Transformed T Cells

Cook, Heidi L.; Mischo, Hannah E.; Steitz, Joan A.

doi:10.1128/mcb.24.10.4522-4533.2004

Cited by 45 publications

(49 citation statements)

References 83 publications

(105 reference statements)

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“…To demonstrate that the interaction of AUF1 with EBER1 occurs in vivo, we used a previously developed method that entails UV crosslinking of intact cells, immunoprecipitation, and washing under stringent conditions (Cook et al 2004). The AUF1 peptide sequence identified by mass spectrometry analysis could not discriminate between the four isoforms, as it lies within the RNA recognition motif II common to all isoforms (Fig.…”

Section: Eber1 Predominantly Interacts With the P40 Isoform Of Auf1 Imentioning

confidence: 99%

AUF1/hnRNP D is a novel protein partner of the EBER1 noncoding RNA of Epstein-Barr virus

Lee

Pimienta

Steitz

2012

RNA

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Epstein-Barr virus (EBV)-infected cells express two noncoding RNAs called EBV-encoded RNA (EBER) 1 and EBER2. Despite their high abundance in the nucleus (about 10 6 copies), the molecular function of these noncoding RNAs has remained elusive. Here, we report that the insertion into EBER1 of an RNA aptamer that binds the bacteriophage MS2 coat protein allows the isolation of EBER1 and associated protein partners. By combining MS2-mediated selection with stable isotope labeling of amino acids in cell culture (SILAC) and analysis by mass spectrometry, we identified AUF1 (AU-rich element binding factor 1)/hnRNP D (heterogeneous nuclear ribonucleoprotein D) as an interacting protein of EBER1. AUF1 exists as four isoforms generated by alternative splicing and is best known for its role in destabilizing mRNAs upon binding to AU-rich elements (AREs) in their 39 untranslated region (UTR). Using UV crosslinking, we demonstrate that predominantly the p40 isoform of AUF1 interacts with EBER1 in vivo. Electrophoretic mobility shift assays show that EBER1 can compete for the binding of the AUF1 p40 isoform to ARE-containing RNA. Given the high abundance of EBER1 in EBV-positive cells, EBER1 may disturb the normal homeostasis between AUF1 and ARE-containing mRNAs or compete with other AUF1-interacting targets in cells latently infected by EBV.

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Section: Eber1 Predominantly Interacts With the P40 Isoform Of Auf1 Imentioning

confidence: 99%

AUF1/hnRNP D is a novel protein partner of the EBER1 noncoding RNA of Epstein-Barr virus

Lee

Pimienta

Steitz

2012

RNA

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“…HSURs are viral RNAs whose functions are currently being investigated (Lee et al 1988;Lee and Steitz 1990;Cook et al 2004Cook et al , 2005. The SMN complex assembles Sm cores on canonical Sm sites contained in each of these RNAs (Golembe et al 2005b).…”

Section: How Does the Smn Complex Identify Snrnas?mentioning

confidence: 99%

The SMN Complex: An Assembly Machine for RNPs

Battle¹,

Kasim²,

Yong³

et al. 2006

Cold Spring Harbor Symposia on Quantitative Biology

169

156

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“…The concept of a recruiter seems logical given the presence of motifs in mRNAs that are associated with mRNA stability and HSUR-1 is degraded by an AU-rich element (ARE)-dependent pathway. 29 However, to date, there are no reports pinning these motifs to miRNA degradation. Little is known about the localization of miRNA turnover, however components of RISC have been shown to be associated with multivesicular bodies (MVB), which have been linked to gene silencing and RISC turnover.…”

Section: Destructive Regulators Of Mirnas: Recruiters Localizers or mentioning

confidence: 99%

RNA-mediated degradation of microRNAs: A widespread viral strategy?

McCaskill

Praihirunkit²,

Sharp

et al. 2015

RNA Biology

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TheHerpesvirus saimiriSmall Nuclear RNAs Recruit AU-Rich Element-Binding Proteins but Do Not Alter Host AU-Rich Element-Containing mRNA Levels in Virally Transformed T Cells

Cited by 45 publications

References 83 publications

AUF1/hnRNP D is a novel protein partner of the EBER1 noncoding RNA of Epstein-Barr virus

AUF1/hnRNP D is a novel protein partner of the EBER1 noncoding RNA of Epstein-Barr virus

The SMN Complex: An Assembly Machine for RNPs

RNA-mediated degradation of microRNAs: A widespread viral strategy?

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