Agrobacterium Counteracts Host-Induced Degradation of Its Effector F-Box Protein

被引:42
作者
Magori, Shimpei [1 ]
Citovsky, Vitaly [1 ]
机构
[1] SUNY Stony Brook, Dept Biochem & Cell Biol, Stony Brook, NY 11794 USA
基金
日本学术振兴会; 美国农业部;
关键词
PLANT GENETIC-TRANSFORMATION; T-DNA; MOLECULAR CHARACTERIZATION; NOPALINE STRAINS; VIRD OPERON; VIRULENCE; TUMEFACIENS; EXPRESSION; COMPLEX; UBIQUITINATION;
D O I
10.1126/scisignal.2002124
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The SCF (Skp1-Cul1-F-box protein) ubiquitin ligase complex plays a pivotal role in various biological processes, including host-pathogen interactions. Many pathogens exploit the host SCF machinery to promote efficient infection by translocating pathogen-encoded F-box proteins into the host cell. How pathogens ensure sufficient amounts of the F-box effectors in the host cell despite the intrinsically unstable nature of F-box proteins, however, remains unclear. We found that the Agrobacterium F-box protein VirF, an important virulence factor, undergoes rapid degradation through the host proteasome pathway. This destabilization of VirF was counteracted by VirD5, another bacterial effector that physically associated with VirF. These observations reveal a previously unknown counterdefense strategy used by pathogens against potential host antimicrobial responses.
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页数:7
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共 42 条
[1]   Ralstonia solanacearum requires F-box-like domain-containing type III effectors to promote disease on several host plants [J].
Angot, Aurelie ;
Peeters, Nemo ;
Lechner, Esther ;
Vailleau, Fabienne ;
Baud, Catherine ;
Gentzbittel, Laurent ;
Sartorel, Elodie ;
Genschik, Pascal ;
Boucher, Christian ;
Genin, Stephane .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (39) :14620-14625
[2]   Clink, a nanovirus-encoded protein, binds both pRB and SKP1 [J].
Aronson, MN ;
Meyer, AD ;
Györgyey, J ;
Katul, L ;
Vetten, HJ ;
Gronenborn, B ;
Timchenko, T .
JOURNAL OF VIROLOGY, 2000, 74 (07) :2967-2972
[3]   Tome-1, a trigger of mitotic entry, is degraded during G1 via the APC [J].
Ayad, NG ;
Rankin, S ;
Murakami, M ;
Jebanathirajah, J ;
Gygi, S ;
Kirschner, MW .
CELL, 2003, 113 (01) :101-113
[4]   The polerovirus silencing suppressor PO targets ARGONAUTE proteins for degradation [J].
Baumberger, Nicolas ;
Tsai, Ching-Hsui ;
Lie, Miranda ;
Havecker, Ericka ;
Baulcombe, David C. .
CURRENT BIOLOGY, 2007, 17 (18) :1609-1614
[5]   The polerovirus F box protein PO targets ARGONAUTE1 to suppress RNA silencing [J].
Bortolamiol, Diane ;
Pazhouhandeh, Maghsoud ;
Marrocco, Katia ;
Genschik, Pascal ;
Ziegler-Graff, Veronique .
CURRENT BIOLOGY, 2007, 17 (18) :1615-1621
[6]   Localizing protein-protein interactions by bimolecular fluorescence complementation in planta [J].
Citovsky, Vitaly ;
Gafni, Yedidya ;
Tzfira, Tzvi .
METHODS, 2008, 45 (03) :196-206
[7]   Biological systems of the host cell involved in Agrobacterium infection [J].
Citovsky, Vitaly ;
Kozlovsky, Stanislav V. ;
Lacroix, Benoit ;
Zaltsman, Adi ;
Dafny-Yelin, Mery ;
Vyas, Shachi ;
Tovkach, Andriy ;
Tzfira, Tzvi .
CELLULAR MICROBIOLOGY, 2007, 9 (01) :9-20
[8]   Proteasomal degradation in plant-pathogen interactions [J].
Citovsky, Vitaly ;
Zaltsman, Adi ;
Kozlovsky, Stanislav V. ;
Gafni, Yedidya ;
Krichevsky, Alexander .
SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY, 2009, 20 (09) :1048-1054
[9]   Direct and indirect roles of viral suppressors of RNA silencing in pathogenesis [J].
Diaz-Pendon, Juan A. ;
Ding, Shou-Wei .
ANNUAL REVIEW OF PHYTOPATHOLOGY, 2008, 46 :303-326
[10]   The Arabidopsis thaliana transcriptome in response to Agrobacterium tumefaciens [J].
Ditt, Renata F. ;
Kerr, Kathleen F. ;
de Figueiredo, Paul ;
Delrow, Jeff ;
Comai, Luca ;
Nester, Eugene W. .
MOLECULAR PLANT-MICROBE INTERACTIONS, 2006, 19 (06) :665-681