HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 276, Issue 23, 19905-19912, June 8, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/23/19905    most recent M009513200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Goodwin, D. J. Articles by Whitehouse, A. Search for Related Content PubMed PubMed Citation Articles by Goodwin, D. J. Articles by Whitehouse, A. Social Bookmarking                      What's this?

A -2 Herpesvirus Nucleocytoplasmic Shuttle Protein Interacts with Importin 1 and 5^*

Delyth J. Goodwin and Adrian Whitehouse^§

From the Molecular Medicine Unit, University of Leeds, St. James's University Hospital, Leeds LS9 7TF, United Kingdom

Herpesvirus saimiri (HVS) is the prototype -2 herpesvirus. This is an increasing important subfamily of herpesviruses due to the identification of the first human -2 herpesvirus, Kaposi's sarcoma-associated herpesvirus. The HVS open reading frame (ORF) 57 protein is a multifunctional trans-regulatory protein homologous to genes identified in all classes of herpesviruses. Recent analysis has demonstrated that ORF 57 has the ability to bind viral RNA and to shuttle between the nucleus and cytoplasm, and is required for efficient nuclear export of viral transcripts. Here we have investigated the nucleocytoplasmic shuttling mechanism utilized by the ORF 57 protein. The yeast two-hybrid system was employed to identify interacting cellular proteins using ORF 57 as bait. We demonstrate that ORF 57 interacts with importin  isoforms 1 and 5. In addition, the binding of ORF 57 to importin  was mediated by the importin  hydrophobic internal armadillo repeats. An ORF 57 amino-terminal arginine-rich sequence, which functions as a nuclear localization sequence, was also required for this interaction. Furthermore, the ORF 57 protein is responsible for the redistribution of importin  into the nucleoli. These results identify novel cellular interactions essential for the functioning of this important herpesvirus regulatory protein.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				K. J. Colgan, J. R. Boyne, and A. Whitehouse Uncoupling of hTREX demonstrates that UAP56 and hTHO-complex recruitment onto herpesvirus saimiri intronless transcripts is required for replication J. Gen. Virol., June 1, 2009; 90(6): 1455 - 1460. [Abstract] [Full Text] [PDF]

				K. J. Colgan, J. R. Boyne, and A. Whitehouse Identification of a response element in a herpesvirus saimiri mRNA recognized by the ORF57 protein J. Gen. Virol., March 1, 2009; 90(3): 596 - 601. [Abstract] [Full Text] [PDF]

				J. R. Boyne and A. Whitehouse Nucleolar trafficking is essential for nuclear export of intronless herpesvirus mRNA PNAS, October 10, 2006; 103(41): 15190 - 15195. [Abstract] [Full Text] [PDF]

				V. Majerciak, K. Yamanegi, S. H. Nie, and Z.-M. Zheng Structural and Functional Analyses of Kaposi Sarcoma-associated Herpesvirus ORF57 Nuclear Localization Signals in Living Cells J. Biol. Chem., September 22, 2006; 281(38): 28365 - 28378. [Abstract] [Full Text] [PDF]

				K. Melen, R. Fagerlund, J. Franke, M. Kohler, L. Kinnunen, and I. Julkunen Importin {alpha} Nuclear Localization Signal Binding Sites for STAT1, STAT2, and Influenza A Virus Nucleoprotein J. Biol. Chem., July 18, 2003; 278(30): 28193 - 28200. [Abstract] [Full Text] [PDF]

				C. C. Lanning, R. Ruiz-Velasco, and C. L. Williams Novel Mechanism of the Co-regulation of Nuclear Transport of SmgGDS and Rac1 J. Biol. Chem., March 28, 2003; 278(14): 12495 - 12506. [Abstract] [Full Text] [PDF]