Multiple Interaction Domains in FtsL, a Protein Component of the Widely Conserved Bacterial FtsLBQ Cell Division Complex

被引:42
作者
Gonzalez, Mark D. [1 ,2 ]
Akbay, Esra A. [3 ,4 ]
Boyd, Dana [1 ]
Beckwith, Jon [1 ]
机构
[1] Harvard Univ, Sch Med, Dept Microbiol & Mol Genet, Boston, MA 02115 USA
[2] Washington Univ, Sch Med, Ctr Genome Sci, St Louis, MO 63108 USA
[3] Univ Texas SW Med Ctr Dallas, Dept Pathol, Dallas, TX 75390 USA
[4] Univ Texas SW Med Ctr Dallas, Simmons Comprehens Canc Ctr, Dallas, TX 75390 USA
关键词
ESCHERICHIA-COLI; BACILLUS-SUBTILIS; SEPTAL LOCALIZATION; GENOME SEQUENCE; DCW CLUSTER; DIVISOME; GENE; DIVIB; COLOCALIZATION; INSTABILITY;
D O I
10.1128/JB.01609-09
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
A bioinformatic analysis of nearly 400 genomes indicates that the overwhelming majority of bacteria possess homologs of the Escherichia coli proteins FtsL, FtsB, and FtsQ, three proteins essential for cell division in that bacterium. These three bitopic membrane proteins form a subcomplex in vivo, independent of the other cell division proteins. Here we analyze the domains of E. coli FtsL that are involved in the interaction with other cell division proteins and important for the assembly of the divisome. We show that FtsL, as we have found previously with FtsB, packs an enormous amount of information in its sequence for interactions with proteins upstream and downstream in the assembly pathway. Given their size, it is likely that the sole function of the complex of these two proteins is to act as a scaffold for divisome assembly.
引用
收藏
页码:2757 / 2768
页数:12
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