Enhancement of Transactivation Activity of Rta of Epstein-Barr Virus by RanBPM

Li Kwan Chang; Shih Tung Liu; Chung Wen Kuo; Wen Hung Wang; Jian Ying Chuang; Elisabetta Bianchi; Yi Ren Hong

doi:10.1016/j.jmb.2008.04.011

Enhancement of Transactivation Activity of Rta of Epstein-Barr Virus by RanBPM

Li Kwan Chang, Shih Tung Liu, Chung Wen Kuo, Wen Hung Wang, Jian Ying Chuang, Elisabetta Bianchi, Yi Ren Hong

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

38 Citations (Scopus)

Abstract

Epstein-Barr virus (EBV) expresses the immediate-early protein Rta to activate the transcription of EBV lytic genes and the lytic cycle. We show that RanBPM acts as a binding partner of Rta in yeast two-hybrid analysis. The binding was confirmed by glutathione-S-transferase pull-down assay. A coimmunoprecipitation experiment and confocal microscopy revealed that RanBPM and Rta interact in vivo and colocalize in the nucleus. The interaction appears to involve the SPRY domain in RanBPM and the region between amino acid residues 416 to 476 in Rta. The interaction promotes the transactivation activity of Rta in activating the transcription of BMLF1 and p21 in transient transfection assays. Additionally, RanBPM interacts with SUMO-E2 (Ubc9) to promote sumoylation of Rta by SUMO-1. This fact explains why the expression of RanBPM enhances the transactivation activity of Rta. Taken together, the present results indicate a new role of RanBPM in regulating a viral protein that is critical to EBV lytic activation.

Original language	English
Pages (from-to)	231-242
Number of pages	12
Journal	Journal of Molecular Biology
Volume	379
Issue number	2
DOIs	https://doi.org/10.1016/j.jmb.2008.04.011
Publication status	Published - May 29 2008
Externally published	Yes

Keywords

Epstein-Barr virus
RanBPM
Rta

ASJC Scopus subject areas

Biophysics
Structural Biology
Molecular Biology

Access to Document

10.1016/j.jmb.2008.04.011

Cite this

@article{8e43247b3e954b0ca25a0e30f3c9731b,

title = "Enhancement of Transactivation Activity of Rta of Epstein-Barr Virus by RanBPM",

abstract = "Epstein-Barr virus (EBV) expresses the immediate-early protein Rta to activate the transcription of EBV lytic genes and the lytic cycle. We show that RanBPM acts as a binding partner of Rta in yeast two-hybrid analysis. The binding was confirmed by glutathione-S-transferase pull-down assay. A coimmunoprecipitation experiment and confocal microscopy revealed that RanBPM and Rta interact in vivo and colocalize in the nucleus. The interaction appears to involve the SPRY domain in RanBPM and the region between amino acid residues 416 to 476 in Rta. The interaction promotes the transactivation activity of Rta in activating the transcription of BMLF1 and p21 in transient transfection assays. Additionally, RanBPM interacts with SUMO-E2 (Ubc9) to promote sumoylation of Rta by SUMO-1. This fact explains why the expression of RanBPM enhances the transactivation activity of Rta. Taken together, the present results indicate a new role of RanBPM in regulating a viral protein that is critical to EBV lytic activation.",

keywords = "Epstein-Barr virus, RanBPM, Rta",

author = "Chang, {Li Kwan} and Liu, {Shih Tung} and Kuo, {Chung Wen} and Wang, {Wen Hung} and Chuang, {Jian Ying} and Elisabetta Bianchi and Hong, {Yi Ren}",

note = "Funding Information: Dr Takeharu Nishimoto in Kyushu University is appreciated for providing an RanBPM plasmid. Dr. T.-Y. Hsu is appreciated for providing pEGFP-Rta. This research was supported by the National Health Research Institute of the Republic of China, Taiwan (contract no. NHRI-EX95-9503BC) and the National Science Council of the Republic of China, Taiwan (contract no. NSC95-3112-B-182-002). ",

year = "2008",

month = may,

day = "29",

doi = "10.1016/j.jmb.2008.04.011",

language = "English",

volume = "379",

pages = "231--242",

journal = "Journal of Molecular Biology",

issn = "0022-2836",

publisher = "Academic Press",

number = "2",

}

TY - JOUR

T1 - Enhancement of Transactivation Activity of Rta of Epstein-Barr Virus by RanBPM

AU - Chang, Li Kwan

AU - Liu, Shih Tung

AU - Kuo, Chung Wen

AU - Wang, Wen Hung

AU - Chuang, Jian Ying

AU - Bianchi, Elisabetta

AU - Hong, Yi Ren

N1 - Funding Information: Dr Takeharu Nishimoto in Kyushu University is appreciated for providing an RanBPM plasmid. Dr. T.-Y. Hsu is appreciated for providing pEGFP-Rta. This research was supported by the National Health Research Institute of the Republic of China, Taiwan (contract no. NHRI-EX95-9503BC) and the National Science Council of the Republic of China, Taiwan (contract no. NSC95-3112-B-182-002).

PY - 2008/5/29

Y1 - 2008/5/29

N2 - Epstein-Barr virus (EBV) expresses the immediate-early protein Rta to activate the transcription of EBV lytic genes and the lytic cycle. We show that RanBPM acts as a binding partner of Rta in yeast two-hybrid analysis. The binding was confirmed by glutathione-S-transferase pull-down assay. A coimmunoprecipitation experiment and confocal microscopy revealed that RanBPM and Rta interact in vivo and colocalize in the nucleus. The interaction appears to involve the SPRY domain in RanBPM and the region between amino acid residues 416 to 476 in Rta. The interaction promotes the transactivation activity of Rta in activating the transcription of BMLF1 and p21 in transient transfection assays. Additionally, RanBPM interacts with SUMO-E2 (Ubc9) to promote sumoylation of Rta by SUMO-1. This fact explains why the expression of RanBPM enhances the transactivation activity of Rta. Taken together, the present results indicate a new role of RanBPM in regulating a viral protein that is critical to EBV lytic activation.

AB - Epstein-Barr virus (EBV) expresses the immediate-early protein Rta to activate the transcription of EBV lytic genes and the lytic cycle. We show that RanBPM acts as a binding partner of Rta in yeast two-hybrid analysis. The binding was confirmed by glutathione-S-transferase pull-down assay. A coimmunoprecipitation experiment and confocal microscopy revealed that RanBPM and Rta interact in vivo and colocalize in the nucleus. The interaction appears to involve the SPRY domain in RanBPM and the region between amino acid residues 416 to 476 in Rta. The interaction promotes the transactivation activity of Rta in activating the transcription of BMLF1 and p21 in transient transfection assays. Additionally, RanBPM interacts with SUMO-E2 (Ubc9) to promote sumoylation of Rta by SUMO-1. This fact explains why the expression of RanBPM enhances the transactivation activity of Rta. Taken together, the present results indicate a new role of RanBPM in regulating a viral protein that is critical to EBV lytic activation.

KW - Epstein-Barr virus

KW - RanBPM

KW - Rta

UR - http://www.scopus.com/inward/record.url?scp=43049127401&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=43049127401&partnerID=8YFLogxK

U2 - 10.1016/j.jmb.2008.04.011

DO - 10.1016/j.jmb.2008.04.011

M3 - Article

C2 - 18455188

AN - SCOPUS:43049127401

SN - 0022-2836

VL - 379

SP - 231

EP - 242

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 2

ER -

Enhancement of Transactivation Activity of Rta of Epstein-Barr Virus by RanBPM

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this