Interaction between basic residues of epstein-barr virus EBNA1 protein and cellular chromatin mediates viral plasmid maintenance

Teru Kanda; Naoki Horikoshi; Takayuki Murata; Daisuke Kawashima; Atsuko Sugimoto; Yohei Narita; Hitoshi Kurumizaka; Tatsuya Tsurumi

doi:10.1074/jbc.M113.491167

Interaction between basic residues of epstein-barr virus EBNA1 protein and cellular chromatin mediates viral plasmid maintenance

Teru Kanda^*, Naoki Horikoshi, Takayuki Murata, Daisuke Kawashima, Atsuko Sugimoto, Yohei Narita, Hitoshi Kurumizaka, Tatsuya Tsurumi

^*Corresponding author for this work

Waseda Research Institute for Science and Engineering

Research output: Contribution to journal › Article › peer-review

16 Citations (Scopus)

Abstract

Background: Epstein-Barr virus episomes piggyback onto cellular chromosomes in latently infected cells. Results: EBNA1 was functionally sound even when arginines within its chromosome binding domains were replaced with lysines. Conclusion: The basic nature of the domains is critically important for the chromosome binding. Significance: Learning how EBNA1 attaches to chromosomes is crucial for understanding the mechanism of stable maintenance of viral episomes.

Original language	English
Pages (from-to)	24189-24199
Number of pages	11
Journal	Journal of Biological Chemistry
Volume	288
Issue number	33
DOIs	https://doi.org/10.1074/jbc.M113.491167
Publication status	Published - 2013 Aug 16

ASJC Scopus subject areas

Biochemistry
Cell Biology
Molecular Biology

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title = "Interaction between basic residues of epstein-barr virus EBNA1 protein and cellular chromatin mediates viral plasmid maintenance",

abstract = "Background: Epstein-Barr virus episomes piggyback onto cellular chromosomes in latently infected cells. Results: EBNA1 was functionally sound even when arginines within its chromosome binding domains were replaced with lysines. Conclusion: The basic nature of the domains is critically important for the chromosome binding. Significance: Learning how EBNA1 attaches to chromosomes is crucial for understanding the mechanism of stable maintenance of viral episomes.",

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doi = "10.1074/jbc.M113.491167",

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AU - Kanda, Teru

AU - Horikoshi, Naoki

AU - Murata, Takayuki

AU - Kawashima, Daisuke

AU - Sugimoto, Atsuko

AU - Narita, Yohei

AU - Kurumizaka, Hitoshi

AU - Tsurumi, Tatsuya

PY - 2013/8/16

Y1 - 2013/8/16

N2 - Background: Epstein-Barr virus episomes piggyback onto cellular chromosomes in latently infected cells. Results: EBNA1 was functionally sound even when arginines within its chromosome binding domains were replaced with lysines. Conclusion: The basic nature of the domains is critically important for the chromosome binding. Significance: Learning how EBNA1 attaches to chromosomes is crucial for understanding the mechanism of stable maintenance of viral episomes.

AB - Background: Epstein-Barr virus episomes piggyback onto cellular chromosomes in latently infected cells. Results: EBNA1 was functionally sound even when arginines within its chromosome binding domains were replaced with lysines. Conclusion: The basic nature of the domains is critically important for the chromosome binding. Significance: Learning how EBNA1 attaches to chromosomes is crucial for understanding the mechanism of stable maintenance of viral episomes.

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JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 33

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Interaction between basic residues of epstein-barr virus EBNA1 protein and cellular chromatin mediates viral plasmid maintenance

Abstract

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