Bacterial Division Proteins FtsZ and ZipA Induce Vesicle Shrinkage and Cell Membrane Invagination

被引：52

作者：

Cabre, Elisa J. ^{[1
]}

Sanchez-Gorostiaga, Alicia ^{[2
]}

Carrara, Paolo ^{[3
]}

Ropero, Noelia ^{[1
]}

Casanova, Mercedes ^{[2
]}

Palacios, Pilar ^{[2
]}

Stano, Pasquale ^{[3
]}

Jimenez, Mercedes ^{[1
]}

Rivas, German ^{[1
]}

Vicente, Miguel ^{[2
]}

机构：

[1] CSIC, CIB, E-28040 Madrid, Spain

[2] CSIC, Ctr Nacl Biotecnol, Madrid 28049, Spain

[3] Univ Roma Tre, Dipartimento Biol, I-00146 Rome, Italy

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2013年 / 288卷 / 37期

关键词：

ESCHERICHIA-COLI; GIANT VESICLES; SEPTAL RING; ACTIN; RECONSTITUTION; LIPOSOMES; PROTOFILAMENTS; MORPHOGENESIS; RECRUITMENT; SEQUENCE;

D O I：

10.1074/jbc.M113.491688

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：

Permeable vesicles containing the proto-ring anchoring ZipA protein shrink when FtsZ, the main cell division protein, polymerizes in the presence of GTP. Shrinkage, resembling the constriction of the cytoplasmic membrane, occurs at ZipA densities higher than those found in the cell and is modulated by the dynamics of the FtsZ polymer. In vivo, an excess of ZipA generates multilayered membrane inclusions within the cytoplasm and causes the loss of the membrane function as a permeability barrier. Overproduction of ZipA at levels that block septation is accompanied by the displacement of FtsZ and two additional division proteins, FtsA and FtsN, from potential septation sites to clusters that colocalize with ZipA near the membrane. The results show that elementary constriction events mediated by defined elements involved in cell division can be evidenced both in bacteria and in vesicles.

引用

页码：26625 / 26634

页数：10

共 52 条

[1] Bacterial cell division: assembly, maintenance and disassembly of the Z ring [J].