J Gen Virol Email Content Delivery
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by López, L.
Right arrow Articles by García, J. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by López, L.
Right arrow Articles by García, J. A.
Agricola
Right arrow Articles by López, L.
Right arrow Articles by García, J. A.
Journal of General Virology (2001), 82, 677-686.
© 2001 Society for General Microbiology

Plant

Identification of an N-terminal domain of the plum pox potyvirus CI RNA helicase involved in self-interaction in a yeast two-hybrid system

Lissett López1, Ana Urzainquib,1, Elvira Domínguez1 and Juan Antonio García1

Centro Nacional de Biotecnología (CSIC), Campus de la Universidad Autónoma de Madrid, 28049 Madrid, Spain1

Author for correspondence: Juan Antonio García. Fax +34 915854535. e-mail jagarcia{at}cnb.uam.es

Potyvirus CI RNA helicase is a protein involved in RNA genome replication and virus movement. The protein aggregates in the cytoplasm of infected cells to form typical cylindrical inclusions. A yeast two-hybrid system was used to analyse interactions of the CI RNA helicase from plum pox potyvirus (PPV) with itself and with other viral proteins. No interactions could be detected of full-length CI protein with itself or with PPV P3/6K1, NIa, NIb or CP proteins. However, positive self-interactions were detected for N-terminal fragments of the CI protein, allowing the mapping of a CI–CI binding domain to the N-terminal 177 aa of the protein. Further deletion analysis suggested that several regions of this domain contribute to the interaction. Moreover, pull-down experiments demonstrate that, at least in vitro, full-length PPV CI protein is able to self-interact in the absence of other virus or plant factors.




This article has been cited by other articles:


Home page
 J. Gen. Virol.Home page
R. Gabrenaite-Verkhovskaya, I. A. Andreev, N. O. Kalinina, L. Torrance, M. E. Taliansky, and K. Makinen
Cylindrical inclusion protein of potato virus A is associated with a subpopulation of particles isolated from infected plants
J. Gen. Virol., March 1, 2008; 89(3): 829 - 838.
[Abstract] [Full Text] [PDF]

Home page
 J Electron Microsc (Tokyo)Home page
B. Zechmann, M. Muller, and G. Zellnig
Effects of different fixation and freeze substitution methods on the ultrastructural preservation of ZYMV-infected Cucurbita pepo (L.) leaves
J. Electron Microsc. (Tokyo), August 1, 2005; 54(4): 393 - 402.
[Abstract] [Full Text] [PDF]

Home page
 J. Gen. Virol.Home page
Ma. L. M. Yambao, C. Masuta, K. Nakahara, and I. Uyeda
The central and C-terminal domains of VPg of Clover yellow vein virus are important for VPg-HCPro and VPg-VPg interactions
J. Gen. Virol., October 1, 2003; 84(10): 2861 - 2869.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2001 by the Society for General Microbiology.