Subcellular positioning of F plasmid mediated by dynamic localization of SopA and SopB

被引:66
作者
Adachi, S
Hori, K
Hiraga, S [1 ]
机构
[1] Kyoto Univ, Grad Sch Med, Dept Radiat Genet, Sakyo Ku, Kyoto 6068501, Japan
[2] Kyoto Univ, Grad Sch Engn, Dept Civil & Earth Resources Engn, Sakyo Ku, Kyoto 6068501, Japan
基金
日本学术振兴会;
关键词
F plasmid; plasmid positioning; oscillation of protein; reaction-diffusion system; plasmid incompatibility;
D O I
10.1016/j.jmb.2005.11.088
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
SopA, SopB proteins and the cis-acting sopC DNA region of F plasmid are essential for partitioning of the plasmid, ensuring proper subcellular positioning of the plasmid DNA molecules. We have analyzed by immunofluorescence microscopy the subcellular localization of SopA and SopB. The majority of SopB molecules formed foci, which localized frequently with F plasmid DNA molecules. The foci increased in number in proportion to the cell length. Interestingly, beside the foci formation, SopB formed a spiral structure that was dependent on SopA, which also formed a spiral structure, independent of the presence of SopB, and these two structures partially overlapped. On the basis of these results and previous biochemical studies together with our simulations, we propose a theoretical model named "the reaction-diffusion partitioning model", using reaction-diffusion equations that explain the dynamic subcellular localization of SopA and SopB proteins and the subcellular positioning of F plasmid. We hypothesized that sister copies of plasmid DNA compete with each other for sites at which SopB multimer is at the optimum concentration. The plasmid incompatibility mediated by the Sop system might be explained clearly by this hypothesis. (c) 2005 Elsevier Ltd. All rights reserved.
引用
收藏
页码:850 / 863
页数:14
相关论文
共 52 条
[1]   PARTITION-MEDIATED INCOMPATIBILITY OF BACTERIAL PLASMIDS [J].
AUSTIN, S ;
NORDSTROM, K .
CELL, 1990, 60 (03) :351-354
[2]   Bacterial DNA segregation dynamics mediated by the polymerizing protein ParF [J].
Barillá, D ;
Rosenberg, MF ;
Nobbmann, U ;
Hayes, F .
EMBO JOURNAL, 2005, 24 (07) :1453-1464
[3]   Probing plasmid partition with centromere-based incompatibility [J].
Bouet, JY ;
Rech, J ;
Egloff, S ;
Biek, DP ;
Lane, D .
MOLECULAR MICROBIOLOGY, 2005, 55 (02) :511-525
[4]   P1 ParA interacts with the P1 partition complex at parS and an ATP-ADP switch controls ParA activities [J].
Bouet, JY ;
Funnell, BE .
EMBO JOURNAL, 1999, 18 (05) :1415-1424
[5]  
DAVEY MJ, 1994, J BIOL CHEM, V269, P29908
[6]   BIOCHEMICAL ACTIVITIES OF THE PARA PARTITION PROTEIN OF THE P1 PLASMID [J].
DAVIS, MA ;
MARTIN, KA ;
AUSTIN, SJ .
MOLECULAR MICROBIOLOGY, 1992, 6 (09) :1141-1147
[7]   RECOGNITION OF THE P1 PLASMID CENTROMERE ANALOG INVOLVES BINDING OF THE PARB PROTEIN AND IS MODIFIED BY A SPECIFIC HOST FACTOR [J].
DAVIS, MA ;
AUSTIN, SJ .
EMBO JOURNAL, 1988, 7 (06) :1881-1888
[8]   Arp2/3 complex requires hydrolyzable ATP for nucleation of new actin filaments [J].
Dayel, MJ ;
Holleran, EA ;
Mullins, RD .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (26) :14871-14876
[9]   Stochastic model for Soj relocation dynamics in Bacillus subtilis [J].
Doubrovinski, K ;
Howard, M .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (28) :9808-9813
[10]   A polymerization-depolymerization model that accurately generates the self-sustained oscillatory system involved in bacterial division site placement [J].
Drew, DA ;
Osborn, MJ ;
Rothfield, LI .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (17) :6114-6118