Ubiquitination of tombusvirus p33 replication protein plays a role in virus replication and binding to the host Vps23p ESCRT protein

Daniel Barajas; Peter D. Nagy

doi:10.1016/j.virol.2009.11.010

Ubiquitination of tombusvirus p33 replication protein plays a role in virus replication and binding to the host Vps23p ESCRT protein

Daniel Barajas, Peter D. Nagy

Plant Pathology

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

76 Scopus citations

Abstract

Post-translational modifications of viral replication proteins could be widespread phenomena during the replication of plus-stranded RNA viruses. In this article, we identify two lysines in the tombusvirus p33 replication co-factor involved in ubiquitination and show that the same lysines are also important for the p33 to interact with the host Vps23p ESCRT-I factor. We find that the interaction of p33 with Vps23p is also affected by a "late-domain"-like sequence in p33. The combined mutations of the two lysines and the late-domain-like sequences in p33 reduced replication of a replicon RNA of Tomato bushy stunt virus in yeast model host, in plant protoplasts, and plant leaves, suggesting that p33-Vps23p ESCRT protein interaction affects tombusvirus replication. Using ubiquitin-mimicking p33 chimeras, we demonstrate that high level of p33 ubiquitination is inhibitory for TBSV replication. These findings argue that optimal level of p33 ubiquitination plays a regulatory role during tombusvirus infections.

Original language	English
Pages (from-to)	358-368
Number of pages	11
Journal	Virology
Volume	397
Issue number	2
DOIs	https://doi.org/10.1016/j.virol.2009.11.010
State	Published - Feb 20 2010

Bibliographical note

Funding Information:
We thank Drs. Judit Pogany and Zhenghe Li for critical reading of the manuscript and for their very helpful suggestions. The authors thank Dr. Scott D. Emr, Cornell University, for the yeast strains and plasmids. This work was supported by NIH-NIAID (5R21AI072170-02) and by the Kentucky Tobacco Research and Development Center at the University of Kentucky , awarded to P.D.N. D. Barajas was supported in part by a postdoctoral fellowship from the Spanish Ministry of Education and Science.

Keywords

ESCRT
Nicotiana benthamiana
RNA
Replication
Tobacco
Tomato bushy stunt virus
Ubiquitin
Yeast

ASJC Scopus subject areas

Virology

Access to Document

10.1016/j.virol.2009.11.010

Cite this

@article{37c8a4eda5dc48f798adc76fb4313016,

title = "Ubiquitination of tombusvirus p33 replication protein plays a role in virus replication and binding to the host Vps23p ESCRT protein",

abstract = "Post-translational modifications of viral replication proteins could be widespread phenomena during the replication of plus-stranded RNA viruses. In this article, we identify two lysines in the tombusvirus p33 replication co-factor involved in ubiquitination and show that the same lysines are also important for the p33 to interact with the host Vps23p ESCRT-I factor. We find that the interaction of p33 with Vps23p is also affected by a {"}late-domain{"}-like sequence in p33. The combined mutations of the two lysines and the late-domain-like sequences in p33 reduced replication of a replicon RNA of Tomato bushy stunt virus in yeast model host, in plant protoplasts, and plant leaves, suggesting that p33-Vps23p ESCRT protein interaction affects tombusvirus replication. Using ubiquitin-mimicking p33 chimeras, we demonstrate that high level of p33 ubiquitination is inhibitory for TBSV replication. These findings argue that optimal level of p33 ubiquitination plays a regulatory role during tombusvirus infections.",

keywords = "ESCRT, Nicotiana benthamiana, RNA, Replication, Tobacco, Tomato bushy stunt virus, Ubiquitin, Yeast",

author = "Daniel Barajas and Nagy, {Peter D.}",

note = "Funding Information: We thank Drs. Judit Pogany and Zhenghe Li for critical reading of the manuscript and for their very helpful suggestions. The authors thank Dr. Scott D. Emr, Cornell University, for the yeast strains and plasmids. This work was supported by NIH-NIAID (5R21AI072170-02) and by the Kentucky Tobacco Research and Development Center at the University of Kentucky , awarded to P.D.N. D. Barajas was supported in part by a postdoctoral fellowship from the Spanish Ministry of Education and Science.",

year = "2010",

month = feb,

day = "20",

doi = "10.1016/j.virol.2009.11.010",

language = "English",

volume = "397",

pages = "358--368",

number = "2",

}

TY - JOUR

T1 - Ubiquitination of tombusvirus p33 replication protein plays a role in virus replication and binding to the host Vps23p ESCRT protein

AU - Barajas, Daniel

AU - Nagy, Peter D.

N1 - Funding Information: We thank Drs. Judit Pogany and Zhenghe Li for critical reading of the manuscript and for their very helpful suggestions. The authors thank Dr. Scott D. Emr, Cornell University, for the yeast strains and plasmids. This work was supported by NIH-NIAID (5R21AI072170-02) and by the Kentucky Tobacco Research and Development Center at the University of Kentucky , awarded to P.D.N. D. Barajas was supported in part by a postdoctoral fellowship from the Spanish Ministry of Education and Science.

PY - 2010/2/20

Y1 - 2010/2/20

N2 - Post-translational modifications of viral replication proteins could be widespread phenomena during the replication of plus-stranded RNA viruses. In this article, we identify two lysines in the tombusvirus p33 replication co-factor involved in ubiquitination and show that the same lysines are also important for the p33 to interact with the host Vps23p ESCRT-I factor. We find that the interaction of p33 with Vps23p is also affected by a "late-domain"-like sequence in p33. The combined mutations of the two lysines and the late-domain-like sequences in p33 reduced replication of a replicon RNA of Tomato bushy stunt virus in yeast model host, in plant protoplasts, and plant leaves, suggesting that p33-Vps23p ESCRT protein interaction affects tombusvirus replication. Using ubiquitin-mimicking p33 chimeras, we demonstrate that high level of p33 ubiquitination is inhibitory for TBSV replication. These findings argue that optimal level of p33 ubiquitination plays a regulatory role during tombusvirus infections.

AB - Post-translational modifications of viral replication proteins could be widespread phenomena during the replication of plus-stranded RNA viruses. In this article, we identify two lysines in the tombusvirus p33 replication co-factor involved in ubiquitination and show that the same lysines are also important for the p33 to interact with the host Vps23p ESCRT-I factor. We find that the interaction of p33 with Vps23p is also affected by a "late-domain"-like sequence in p33. The combined mutations of the two lysines and the late-domain-like sequences in p33 reduced replication of a replicon RNA of Tomato bushy stunt virus in yeast model host, in plant protoplasts, and plant leaves, suggesting that p33-Vps23p ESCRT protein interaction affects tombusvirus replication. Using ubiquitin-mimicking p33 chimeras, we demonstrate that high level of p33 ubiquitination is inhibitory for TBSV replication. These findings argue that optimal level of p33 ubiquitination plays a regulatory role during tombusvirus infections.

KW - ESCRT

KW - Nicotiana benthamiana

KW - RNA

KW - Replication

KW - Tobacco

KW - Tomato bushy stunt virus

KW - Ubiquitin

KW - Yeast

UR - http://www.scopus.com/inward/record.url?scp=75749102524&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=75749102524&partnerID=8YFLogxK

U2 - 10.1016/j.virol.2009.11.010

DO - 10.1016/j.virol.2009.11.010

M3 - Article

C2 - 20004458

AN - SCOPUS:75749102524

SN - 0042-6822

VL - 397

SP - 358

EP - 368

JO - Virology

JF - Virology

IS - 2

ER -

Ubiquitination of tombusvirus p33 replication protein plays a role in virus replication and binding to the host Vps23p ESCRT protein

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this