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Nucleolin is important for Epstein-Barr virus nuclear antigen 1-mediated episome binding, maintenance, and transcription.

Epstein--Barr virus (EBV) nuclear antigen 1 (EBNA1) is essential for EBV episome maintenance, replication, and transcription. These effects are mediated by EBNA1 binding to cognate oriP DNA, which comprise 20 imperfect copies of a 30-bp dyad symmetry enhancer and an origin for DNA replication. To id... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States of America January 7, 2014, Vol.111(1), pp.243-248
Main Author: Chen, Ya-Lin
Other Authors: Liu, Cheng-Der , Cheng, Chi-Ping , Zhao, Bo , Hsu, Hao-Jen , Shen, Chih-Long , Chiu, Shu-Jun , Kieff, Elliott , Peng, Chih-Wen
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1321800111
Link: http://search.proquest.com/docview/1490751621/?pq-origsite=primo
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recordid: proquest1490751621
title: Nucleolin is important for Epstein-Barr virus nuclear antigen 1-mediated episome binding, maintenance, and transcription.
format: Article
creator:
  • Chen, Ya-Lin
  • Liu, Cheng-Der
  • Cheng, Chi-Ping
  • Zhao, Bo
  • Hsu, Hao-Jen
  • Shen, Chih-Long
  • Chiu, Shu-Jun
  • Kieff, Elliott
  • Peng, Chih-Wen
subjects:
  • Adenosine Triphosphate–Chemistry
  • Binding Sites–Metabolism
  • Cell Line, Tumor–Chemistry
  • Cell Nucleus–Chemistry
  • Chromatography, Liquid–Physiology
  • DNA Replication–Metabolism
  • Epitopes–Metabolism
  • Epstein-Barr Virus Nuclear Antigens–Chemistry
  • Gene Expression Regulation–Physiology
  • Gene Silencing–Metabolism
  • Genome–Chemistry
  • Green Fluorescent Proteins–Physiology
  • Humans–Physiology
  • Immunoprecipitation–Physiology
  • Luciferases–Physiology
  • Mass Spectrometry–Physiology
  • Microscopy, Confocal–Physiology
  • Phosphoproteins–Physiology
  • Plasmids–Physiology
  • Protein Binding
ispartof: Proceedings of the National Academy of Sciences of the United States of America, January 7, 2014, Vol.111(1), pp.243-248
description: Epstein--Barr virus (EBV) nuclear antigen 1 (EBNA1) is essential for EBV episome maintenance, replication, and transcription. These effects are mediated by EBNA1 binding to cognate oriP DNA, which comprise 20 imperfect copies of a 30-bp dyad symmetry enhancer and an origin for DNA replication. To identify cell proteins essential for these EBNA1 functions, EBNA1 associated cell proteins were immune precipitated and analyzed by liquid chromatography-tandem mass spectrometry. Nucleolin (NCL) was identified to be EBNA1 associated. EBNA1's N-terminal 100 aa and NCL's RNA-binding domains were critical for EBNA1/NCL interaction. Lentivirus shRNA-mediated NCL depletion substantially reduced EBNA1 recruitment to oriP DNA, EBNA1-dependent transcription of an EBV oriP luciferase reporter, and EBV genome maintenance in lymphoblastoid cell lines. NCL RNA-binding domain [K.sub.429] was critical for ATP and EBNA1 binding. NCL overexpression increased EBNA1 binding to oriP and transcription, whereas NCL [K.sub.429]A was deficient. Moreover, NCL silencing impaired lymphoblastoid cell line growth. These experiments reveal a surprisingly critical role for NCL K429 in EBNA1 episome maintenance and transcription, which may be a target for therapeutic intervention. lymphoma | chromatin | oncogenic herpesvirus | nasopharyngeal carcinoma www.pnas.org/cgi/doi/10.1073/pnas.1321800111
language: eng
source:
identifier: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1321800111
fulltext: fulltext
issn:
  • 10916490
  • 1091-6490
url: Link


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titleNucleolin is important for Epstein-Barr virus nuclear antigen 1-mediated episome binding, maintenance, and transcription.
creatorChen, Ya-Lin ; Liu, Cheng-Der ; Cheng, Chi-Ping ; Zhao, Bo ; Hsu, Hao-Jen ; Shen, Chih-Long ; Chiu, Shu-Jun ; Kieff, Elliott ; Peng, Chih-Wen
contributorChen, Ya-Lin (correspondence author) ; Chen, Ya-Lin (record owner)
ispartofProceedings of the National Academy of Sciences of the United States of America, January 7, 2014, Vol.111(1), pp.243-248
identifierE-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1321800111
subjectAdenosine Triphosphate–Chemistry ; Binding Sites–Metabolism ; Cell Line, Tumor–Chemistry ; Cell Nucleus–Chemistry ; Chromatography, Liquid–Physiology ; DNA Replication–Metabolism ; Epitopes–Metabolism ; Epstein-Barr Virus Nuclear Antigens–Chemistry ; Gene Expression Regulation–Physiology ; Gene Silencing–Metabolism ; Genome–Chemistry ; Green Fluorescent Proteins–Physiology ; Humans–Physiology ; Immunoprecipitation–Physiology ; Luciferases–Physiology ; Mass Spectrometry–Physiology ; Microscopy, Confocal–Physiology ; Phosphoproteins–Physiology ; Plasmids–Physiology ; Protein Binding
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descriptionEpstein--Barr virus (EBV) nuclear antigen 1 (EBNA1) is essential for EBV episome maintenance, replication, and transcription. These effects are mediated by EBNA1 binding to cognate oriP DNA, which comprise 20 imperfect copies of a 30-bp dyad symmetry enhancer and an origin for DNA replication. To identify cell proteins essential for these EBNA1 functions, EBNA1 associated cell proteins were immune precipitated and analyzed by liquid chromatography-tandem mass spectrometry. Nucleolin (NCL) was identified to be EBNA1 associated. EBNA1's N-terminal 100 aa and NCL's RNA-binding domains were critical for EBNA1/NCL interaction. Lentivirus shRNA-mediated NCL depletion substantially reduced EBNA1 recruitment to oriP DNA, EBNA1-dependent transcription of an EBV oriP luciferase reporter, and EBV genome maintenance in lymphoblastoid cell lines. NCL RNA-binding domain [K.sub.429] was critical for ATP and EBNA1 binding. NCL overexpression increased EBNA1 binding to oriP and transcription, whereas NCL [K.sub.429]A was deficient. Moreover, NCL silencing impaired lymphoblastoid cell line growth. These experiments reveal a surprisingly critical role for NCL K429 in EBNA1 episome maintenance and transcription, which may be a target for therapeutic intervention. lymphoma | chromatin | oncogenic herpesvirus | nasopharyngeal carcinoma www.pnas.org/cgi/doi/10.1073/pnas.1321800111
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titleNucleolin is important for Epstein-Barr virus nuclear antigen 1-mediated episome binding, maintenance, and transcription.
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titleNucleolin is important for Epstein-Barr virus nuclear antigen 1-mediated episome binding, maintenance, and transcription.
authorChen, Ya-Lin ; Liu, Cheng-Der ; Cheng, Chi-Ping ; Zhao, Bo ; Hsu, Hao-Jen ; Shen, Chih-Long ; Chiu, Shu-Jun ; Kieff, Elliott ; Peng, Chih-Wen
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