A hypothesis to explain division site selection in Escherichia coli by combining nucleoid occlusion and Min

被引:35
作者
Norris, V [1 ]
Woldringh, C
Mileykovskaya, E
机构
[1] Univ Rouen, Fac Sci & Tech, CNRS,SIMS, FRE 2829,Assemblages Mol Modelisat & Imagerie, F-76821 Mont St Aignan, France
[2] Univ Amsterdam, BioCent Amsterdam, Swammerdam Inst Life Sci, NL-1098 SM Amsterdam, Netherlands
[3] Univ Texas, Sch Med, Dept Biochem & Mol Biol, Houston, TX 77030 USA
来源
FEBS LETTERS | 2004年 / 561卷 / 1-3期
关键词
membrane domain; FtsZ; min; bacterium; cell division;
D O I
10.1016/S0014-5793(04)00135-8
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 positioning of the site of cell division in Escherichia coli results, it is generally believed, from the operation of nucleoid occlusion in combination with the Min system. Nucleoid occlusion prevents division over the nucleoids and directs it by default to the mid-cell region between segregating nucleoids or to polar regions while the Min system prevents division in polar regions. Unresolved questions include how these systems interact to control the earliest known event in division, the assembly at the membrane of the tubulin-like protein, FtsZ, and, more importantly, what exactly constitutes a division site. Evidence exists that (1) the coupled transcription, translation and insertion of proteins into membrane (transertion), can structure the cytoplasmic membrane into phospholipid domains, (2) the MinD protein can convert vesicles into tubes and (3) a variety of membranous structures can be observed at mid-cell. These data support a model in which transertion from the segregating daughter chromosomes leads to the formation of a distinct proteolipid domain between them at mid-cell; the composition of this domain allows phospholipid tubes to extend like fingers into the cytoplasm; these tubes then become the substrate for the dynamic assembly and disassembly of FtsZ which converts them into the invaginating fold responsible for division; the Min system inhibits division at unwanted sites and times by removing these tubes especially at the cell poles. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:3 / 10
页数:8
相关论文
共 84 条
[51]   Pattern formation in Escherichia coli: A model for the pole-to-pole oscillations of Min proteins and the localization of the division site [J].
Meinhardt, H ;
de Boer, PAJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (25) :14202-14207
[52]   The Min system is not required for precise placement of the midcell Z ring in Bacillus subtilis [J].
Migocki, MD ;
Freeman, MK ;
Wake, RG ;
Harry, EJ .
EMBO REPORTS, 2002, 3 (12) :1163-1167
[53]   Localization and function of early cell division proteins in filamentous Escherichia coli cells lacking phosphatidylethanolamine [J].
Mileykovskaya, E ;
Sun, Q ;
Margolin, W ;
Dowhan, W .
JOURNAL OF BACTERIOLOGY, 1998, 180 (16) :4252-4257
[54]   Visualization of phospholipid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange [J].
Mileykovskaya, E ;
Dowhan, W .
JOURNAL OF BACTERIOLOGY, 2000, 182 (04) :1172-1175
[55]  
MILEYKOVSKAYA E, 2003, J BIOL CHEM, P3200
[56]   Morphogenesis and dynamics of the yeast Golgi apparatus [J].
Morin-Ganet, MN ;
Rambourg, A ;
Deitz, SB ;
Franzusoff, A ;
Képes, F .
TRAFFIC, 2000, 1 (01) :56-68
[57]   AUTORADIOGRAPHIC ANALYSIS OF DIAMINOPIMELIC ACID INCORPORATION IN FILAMENTOUS CELLS OF ESCHERICHIA-COLI - REPRESSION OF PEPTIDOGLYCAN SYNTHESIS AROUND THE NUCLEOID [J].
MULDER, E ;
WOLDRINGH, CL .
JOURNAL OF BACTERIOLOGY, 1991, 173 (15) :4751-4756
[58]   ULTRASTRUCTURE OF THE YEAST ACTIN CYTOSKELETON AND ITS ASSOCIATION WITH THE PLASMA-MEMBRANE [J].
MULHOLLAND, J ;
PREUSS, D ;
MOON, A ;
WONG, A ;
DRUBIN, D ;
BOTSTEIN, D .
JOURNAL OF CELL BIOLOGY, 1994, 125 (02) :381-391
[59]   MESOSOME OF BACILLUS-SUBTILIS AS AFFECTED BY CHEMICAL AND PHYSICAL FIXATION [J].
NANNINGA, N .
JOURNAL OF CELL BIOLOGY, 1971, 48 (01) :219-&
[60]   THE NEW GENE MUKB CODES FOR A 177 KD PROTEIN WITH COILED-COIL DOMAINS INVOLVED IN CHROMOSOME PARTITIONING OF ESCHERICHIA-COLI [J].
NIKI, H ;
JAFFE, A ;
IMAMURA, R ;
OGURA, T ;
HIRAGA, S .
EMBO JOURNAL, 1991, 10 (01) :183-193