Reconstitution of Epstein-Barr virus-based plasmid partitioning in budding yeast

Kapoor, Priya

doi:10.1093/emboj/20.1.222

Cited by 60 publications

(88 citation statements)

References 60 publications

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“…However, although EBNA1 is unlikely to interact with cognate cell DNA to affect cell gene expression or growth, we cannot dismiss the possibility that EBNA1 may interact with cell proteins and affect cells through pathways that may not have been detectable in the experiments described here. EBNA1 N-terminal residues have been implicated in interaction with the cellular proteins p32 and EBP2, and interaction with EBP2 is important in episome persistence (48,49). Also, EBNA1 amino acids 91-321 are a glycine-alanine repeat domain that can inhibit proteasome-mediated degradation of EBNA1 (20).…”

Section: Discussionmentioning

confidence: 99%

Epstein–Barr virus nuclear antigen 1 activates transcription from episomal but not integrated DNA and does not alter lymphocyte growth

Kang

Hung

Kieff

2001

Proc. Natl. Acad. Sci. U.S.A.

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By binding to a cis-acting element (oriP) in the Epstein-Barr virus (EBV)genome, EBV nuclear antigen 1 (EBNA1) enables persistence and enhances transcription from EBV episomes. To investigate whether EBNA1 also directly affects cell gene transcription, we conditionally expressed a Flag-tagged dominant negative EBNA1 (FDNE) in an EBV immortalized lymphoblastoid cell line, in which the EBV genome is integrated into cell DNA. FDNE induction inhibited expression from an EBNA1-dependent oriP reporter plasmid by more than 90% in these cells but did not affect expression from integrated EBV or oriP reporter DNA. FDNE induction also did not alter expression of more than 1,800 cellular mRNAs. Lymphoblastoid cell line growth under a variety of conditions was unaffected by FDNE induction. Although Gal4-VP16 and EBNA1 strongly activated and coactivated a Gal4-VP16-and oriP-dependent promoter that was on an episome, only Gal4-VP16 activated the promoter when it was integrated into chromosomal DNA. These data indicate that EBNA1 is specifically deficient in activation of an integrated oriP enhancer and does not affect cell growth or gene expression through an interaction with cognate chromosomal DNA.

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Section: Discussionmentioning

confidence: 99%

Epstein–Barr virus nuclear antigen 1 activates transcription from episomal but not integrated DNA and does not alter lymphocyte growth

Kang

Hung

Kieff

2001

Proc. Natl. Acad. Sci. U.S.A.

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“…Perhaps the novel 2m CUTs function to regulate the expression of their respective antisense mRNAs in a manner similar to that suggested for GYP5 and its antisense RNA ). Humans contain a single apparent Air protein homolog, ZCCHC7, and segregation of Epstein-Barr virus episomes appears to follow similar rules to that of the yeast 2m plasmid (Kapoor et al 2001;Kapoor and Frappier 2003). Thus it is tempting to speculate that a similar mechanism may govern the inheritance of yeast plasmids and viral genomes in metazoans.…”

Section: à30mentioning

confidence: 99%

Air proteins control differential TRAMP substrate specificity for nuclear RNA surveillance

Schmidt

Mathews

et al. 2012

RNA

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RNA surveillance systems function at critical steps during the formation and function of RNA molecules in all organisms. The RNA exosome plays a central role in RNA surveillance by processing and degrading RNA molecules in the nucleus and cytoplasm of eukaryotic cells. The exosome functions as a complex of proteins composed of a nine-member core and two ribonucleases. The identity of the molecular determinants of exosome RNA substrate specificity remains an important unsolved aspect of RNA surveillance. In the nucleus of Saccharomyces cerevisiae, TRAMP complexes recognize and polyadenylate RNAs, which enhances RNA degradation by the exosome and may contribute to its specificity. TRAMPs contain either of two putative RNA-binding factors called Air proteins. Previous studies suggested that these proteins function interchangeably in targeting the poly(A)-polymerase activity of TRAMPs to RNAs. Experiments reported here show that the Air proteins govern separable functions. Phenotypic analysis and RNA deep-sequencing results from air mutants reveal specific requirements for each Air protein in the regulation of the levels of noncoding and coding RNAs. Loss of these regulatory functions results in specific metabolic and plasmid inheritance defects. These findings reveal differential functions for Air proteins in RNA metabolism and indicate that they control the substrate specificity of the RNA exosome.

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“…This protein was discovered as an EBNA1 binding partner in a two-hybrid screen, and residues 325-376 of EBNA1 are important for this interaction (Shire et al, 1999). It was subsequently shown that EBP2 enables EBNA1 to segregate FR-containing plasmids in yeast by facilitating the interaction of EBNA1 with yeast mitotic chromatin (Kapoor and Frappier, 2003;Kapoor et al, 2001). In keeping with this finding, EBP2 associates with human metaphase chromosomes, and silencing of EBP2 expression results in a large decrease in the amount of EBNA1 associated with metaphase chromosomes (Kapoor et al, 2005;Wu et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Mitotic chromosome interactions of Epstein-Barr nuclear antigen 1 (EBNA1) and human EBNA1-binding protein 2 (EBP2)

Nayyar

Shire

Frappier

2009

Journal of Cell Science

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by tethering the episomes to the cellular chromosomes in mitosis. A host nucleolar protein, EBNA1-binding protein 2 (EBP2), has been shown to be important for interactions between EBNA1 and chromosomes in metaphase and to associate with metaphase chromosomes. Here, we examine the timing of the chromosome associations of EBNA1 and EBP2 through mitosis and the regions of EBNA1 that mediate the chromosome interactions at each stage of mitosis. We show that EBP2 is localized to the nucleolus until late prophase, after which it relocalizes to the chromosome periphery, where it remains throughout telophase. EBNA1 is associated with chromosomes early in prophase through to telophase and partially colocalizes with chromosomal EBP2 in metaphase through to telophase. Using EBNA1 deletion mutants, the chromosome association of EBNA1 at each stage of mitosis was found to be mediated mainly by a central glycinearginine region, and to a lesser degree by N-terminal sequences. These sequence requirements for chromosome interaction mirrored those for EBP2 binding. Our results suggest that interactions between EBNA1 and chromosomes involve at least two stages, and that the contribution of EBP2 to these interactions occurs in the second half of mitosis.

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Reconstitution of Epstein-Barr virus-based plasmid partitioning in budding yeast

Cited by 60 publications

References 60 publications

Epstein–Barr virus nuclear antigen 1 activates transcription from episomal but not integrated DNA and does not alter lymphocyte growth

Epstein–Barr virus nuclear antigen 1 activates transcription from episomal but not integrated DNA and does not alter lymphocyte growth

Air proteins control differential TRAMP substrate specificity for nuclear RNA surveillance

Mitotic chromosome interactions of Epstein-Barr nuclear antigen 1 (EBNA1) and human EBNA1-binding protein 2 (EBP2)

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