In vitro reconstitution of a trimeric complex of DivIB, DivIC and FtsL, and their transient co-localization at the division site in Streptococcus pneumoniae

被引：62

作者：

Noirclerc-Savoye, M

Le Gouëllec, A

Morlot, C

Dideberg, O

Vernet, T

Zapun, A

机构：

[1] CNRS, Inst Biol Struct, CEA, Lab Ingn Macromol,UMR 5075 UJF, F-38027 Grenoble, France

[2] CNRS, Inst Biol Struct, CEA, Lab Cristallogr Macromol,UMR 5075 UJF, F-38027 Grenoble, France

来源：

MOLECULAR MICROBIOLOGY | 2005年 / 55卷 / 02期

关键词：

D O I：

10.1111/j.1365-2958.2004.04408.x

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：

DivIB, DivIC and FtsL are bacterial proteins essential for cell division, which show interdependencies for their stabilities and localization. We have reconstituted in vitro a trimeric complex consisting of the recombinant extracellular domains of the three proteins from Streptococcus pneumoniae. The extracellular domain of DivIB was found to associate with a heterodimer of those of DivIC and FtsL. The heterodimerization of DivIC and FtsL was artificially constrained by fusion with interacting coiled-coils. Immunofluorescence experiments showed that DivIC is always localized at mid-cell, in contrast to DivIB and FtsL, which are co-localized with DivIC only during septation. Taken together, our data suggest that assembly of the trimeric complex DivIB/DivIC/FtsL is regulated during the cell cycle through controlled formation of the DivIC/FtsL heterodimer.

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收藏

页码：413 / 424

页数：12

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