Viral nucleolar localisation signals determine dynamic trafficking within the nucleolus

被引：27

作者：

Emmott, Edward ^{[1
]}

Dove, Brian K. ^{[1
]}

Howell, Gareth ^{[1
]}

Chappell, Lucy A. ^{[1
]}

Reed, Mark L. ^{[1
]}

Boyne, James R. ^{[1
]}

You, Jae-Hwan ^{[1
]}

Brooks, Gavin ^{[2
]}

Whitehouse, Adrian ^{[1
,3
]}

Hiscox, Julian A. ^{[1
,3
]}

机构：

[1] Univ Leeds, Fac Biol Sci, Inst Mol & Cellular Biol, Leeds LS2 9JT, W Yorkshire, England

[2] Univ Reading, Sch Pharm, Reading, Berks, England

[3] Univ Leeds, Astbury Ctr Struct Mol Biol, Leeds LS2 9JT, W Yorkshire, England

来源：

VIROLOGY | 2008年 / 380卷 / 02期

基金：

英国生物技术与生命科学研究理事会; 英国惠康基金;

关键词：

Nucleolus; Nucleolar trafficking; FRAP; FLIP; Herpesvirus; Coronavirus; HIV;

D O I：

10.1016/j.virol.2008.05.032

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Localisation of both viral and cellular proteins to the nucleolus is determined by a variety of factors including nucleolar localisation signals (NoLSs), but how these signals operate is not clearly understood. The nucleolar trafficking of wild type viral proteins and chimeric proteins, which contain altered NoLSs, were compared to investigate the role of NoLSs in dynamic nucleolar trafficking. Three viral proteins from diverse viruses were selected which localised to the nucleolus; the coronavirus infectious bronchitis virus nucleocapsid (N) protein, the herpesvirus saimiri ORF57 protein and the HIV-1 Rev protein. The chimeric proteins were N protein and ORF57 protein which had their own NoLS replaced with those from ORF57 and Rev proteins, respectively. By analysing the sub-cellular localisation and trafficking of these viral proteins and their chimeras within and between nucleoli using confocal microscopy and photo-bleaching we show that NoLSs are responsible for different nucleolar localisations and trafficking rates. (C) 2008 Elsevier Inc. All rights reserved.

引用

页码：191 / 202

页数：12

共 81 条

[1] Nucleolar proteome dynamics [J].

Andersen, JS ;

Lam, YW ;

Leung, AKL ;

Ong, SE ;

Lyon, CE ;

Lamond, AI ;

Mann, M .

NATURE, 2005, 433 (7021) :77-83

[2] Tracking the interactions of rRNA processing proteins during nucleolar assembly in living cells [J].

Angelier, N ;

Tramier, M ;

Louvet, E ;

Coppey-Moisan, M ;

Savino, TM ;

De Mey, JR ;

Hernandez-Verdun, D .

MOLECULAR BIOLOGY OF THE CELL, 2005, 16 (06) :2862-2871

[3] MOBILITY MEASUREMENT BY ANALYSIS OF FLUORESCENCE PHOTOBLEACHING RECOVERY KINETICS [J].

AXELROD, D ;

KOPPEL, DE ;

SCHLESSINGER, J ;

ELSON, E ;

WEBB, WW .

BIOPHYSICAL JOURNAL, 1976, 16 (09) :1055-1069

[4] The conserved N-terminal domain of herpes simplex virus 1 UL24 protein is sufficient to induce the spatial redistribution of nucleolin [J].

Bertrand, Luc ;

Pearson, Angela .

JOURNAL OF GENERAL VIROLOGY, 2008, 89 :1142-1151

[5] Herpesvirus saimiri ORF57: a post-transcriptional regulatory protein [J].

Boyne, James R. ;

Colgan, Kevin J. ;

Whitehouse, Adrian .

FRONTIERS IN BIOSCIENCE-LANDMARK, 2008, 13 :2928-2938

[6] Nucleolar trafficking is essential for nuclear export of intronless herpesvirus mRNA [J].

Boyne, James R. ;

Whitehouse, Adrian .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (41) :15190-15195

[7] To be or not to be in the nucleolus [J].

Carmo-Fonseca, M ;

Mendes-Soares, L ;

Campos, I .

NATURE CELL BIOLOGY, 2000, 2 (06) :E107-E112

[8] The contribution of nuclear compartmentalization to gene regulation [J].

Carmo-Fonseca, M .

CELL, 2002, 108 (04) :513-521

[9] Cell cycle dependent nucleolar localization of the coronavirus nucleocapsid protein [J].

Cawood, Ryan ;

Harrison, Sally M. ;

Dove, Brian K. ;

Reed, Mark L. ;

Hiscox, Julian A. .

CELL CYCLE, 2007, 6 (07) :863-867

[10]

CHANG JH, 1989, J BIOL CHEM, V264, P11732

← 1 2 3 4 5 6 7 8 9 →