The plasmid replicon of Epstein-Barr virus: Mechanistic insights into efficient, licensed, extrachromosomal replication in human cells

被引：85

作者：

Lindner, Scott E. ^{[1
]}

Sugden, Bill ^{[1
]}

机构：

[1] Univ Wisconsin, McArdle Lab Canc Res, Madison, WI 53706 USA

来源：

PLASMID | 2007年 / 58卷 / 01期

关键词：

oriP; EBNA1; EBV; origin; DS; Rep;

D O I：

10.1016/j.plasmid.2007.01.003

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

The genome of Epstein-Barr Virus (EBV) and plasmid derivatives of it are among the most efficient extrachromosomal replicons in mammalian cells. The latent origin of plasmid replication (oriP), when supplied with the viral Epstein-Barr Nuclear Antigen 1 (EBNA1) in trans, provides efficient duplication, partitioning and maintenance of plasmids bearing it. In this review, we detail what is known about the viral cis and trans elements required for plasmid replication. In addition, we describe how the cellular factors that EBV usurps are used to complement the functions of the viral constituents. Finally, we propose a model for the sequential assembly of an EBNA1-dependent origin of DNA synthesis into a pre-Replicative Complex (pre-RC), which functions by making use only of cellular enzymatic activities to carry out the replication of the viral plasmid. (c) 2007 Elsevier Inc. All rights reserved.

引用

页码：1 / 12

页数：12

共 92 条

[11] Replication from oriP of Epstein-Barr virus requires exact spacing of two bound dimers of EBNA1 which bend DNA [J].

Bashaw, JM ;

Yates, JL .

JOURNAL OF VIROLOGY, 2001, 75 (22) :10603-10611

[12] OPTIMAL LENGTHS FOR DNAS ENCAPSIDATED BY EPSTEIN-BARR-VIRUS [J].

BLOSS, TA ;

SUGDEN, B .

JOURNAL OF VIROLOGY, 1994, 68 (12) :8217-8222

[13] Crystal structure of the DNA-Binding domain of the Epstein-Barr virus origin-binding protein, EBNA1, bound to DNA [J].

Bochkarev, A ;

Barwell, JA ;

Pfuetzner, RA ;

Bochkareva, E ;

Frappier, L ;

Edwards, AM .

CELL, 1996, 84 (05) :791-800

[14] BIOLOGICAL SIGNIFICANCE OF UNWINDING CAPABILITY OF NUCLEAR MATRIX ASSOCIATING DNAS [J].

BODE, J ;

KOHWI, Y ;

DICKINSON, L ;

JOH, T ;

KLEHR, D ;

MIELKE, C ;

KOHWISHIGEMATSU, T .

SCIENCE, 1992, 255 (5041) :195-197

[15]

Bogan JA, 2000, J CELL PHYSIOL, V184, P139, DOI 10.1002/1097-4652(200008)184:2<139::AID-JCP1>3.0.CO

[16]

2-8

[17] Human DNA replication initiation factors, ORC and MCM, associate with oriP of Epstein-Barr virus [J].

Chaudhuri, B ;

Xu, HZ ;

Todorov, I ;

Dutta, A ;

Yates, JL .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (18) :10085-10089

[18] Two domains of the Epstein-Barr virus origin DNA-binding protein, EBNA1, orchestrate sequence-specific DNA binding [J].

Cruickshank, J ;

Shire, K ;

Davidson, AR ;

Edwards, AM ;

Frappier, L .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (29) :22273-22277

[19] Inhibition of Epstein-Barr virus OriP function by tankyrase, a telomere-associated poly-ADP ribose polymerase that binds and modifies EBNA1 [J].

Deng, Z ;

Atanasiu, C ;

Zhao, KH ;

Marmorstein, R ;

Sbodio, JI ;

Chi, NW ;

Lieberman, PM .

JOURNAL OF VIROLOGY, 2005, 79 (08) :4640-4650

[20] Telomere repeat binding factors TRF1, TRF2, and hRAP1 modulate replication of Epstein-Barr virus OriP [J].

Deng, Z ;

Atanasiu, C ;

Burg, JS ;

Broccoli, D ;

Lieberman, PM .

JOURNAL OF VIROLOGY, 2003, 77 (22) :11992-12001

← 1 2 3 4 5 6 7 8 9 10 →