RodZ, a component of the bacterial core morphogenic apparatus

被引:129
作者
Alyahya, S. Anisah [1 ,5 ]
Alexander, Roger [1 ,2 ]
Costa, Teresa [4 ]
Henriques, Adriano O. [4 ]
Emonet, Thierry [1 ,3 ]
Jacobs-Wagner, Christine [1 ,5 ,6 ]
机构
[1] Yale Univ, Dept Mol Cellular & Dev Biol, New Haven, CT 06520 USA
[2] Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA
[3] Yale Univ, Dept Phys, New Haven, CT 06520 USA
[4] Univ Nova Lisboa, Inst Tecnol Quim & Biol, Microbial Dev Lab, P-2780157 Oeiras, Portugal
[5] Yale Univ, Sch Med, Sect Microbial Pathogenesis, New Haven, CT 06510 USA
[6] Yale Univ, Howard Hughes Med Inst, New Haven, CT 06520 USA
基金
美国国家卫生研究院;
关键词
cell shape; MreB; cytoskeleton; helix-turn-helix; cell wall; ESCHERICHIA-COLI; CELL-SHAPE; BACILLUS-SUBTILIS; CAULOBACTER-CRESCENTUS; CHROMOSOME SEGREGATION; SEPTUM PLACEMENT; MREB; PROTEINS; WALL; DIVISION;
D O I
10.1073/pnas.0810794106
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The molecular basis of bacterial cell morphogenesis remains largely an open question. Here we discover a morphogenic protein, RodZ, which is widely conserved across the bacterial kingdom. In Caulobacter crescentus, RodZ is essential for viability and is involved in all aspects of this organism's complex morphology. Depletion or over-production of RodZ results in grossly misshapen cells with stalk defects. RodZ exhibits a localization pattern during the cell cycle corresponding to sites of active peptidoglycan synthesis. The temporal transition of RodZ between patchy/helical and mid-cell localization mimics and depends on the actin-like MreB cytoskeleton. In Escherichia coli, an organism with a distinct mode of growth and MreB localization dynamics, RodZ follows MreB and retains its crucial role in cell morphogenesis, demonstrating conservation of function. Genomic analysis shows that RodZ represents an ancient function unique to bacteria. Multiple sequence alignment of 143 RodZ sequences from species across bacterial phyla identifies an N-terminal cytoplasmic domain with a helix-turn-helix motif, a transmembrane sequence, and a previously unidentified, conserved periplasmic or extracellular C-terminal domain. Both the N-and C-terminal domains are important for function, with the N-terminal domain containing localization determinants. This study uncovers a key missing player in the cytoskeleton-based growth machinery enabling heritable and defined cellular forms in bacteria.
引用
收藏
页码:1239 / 1244
页数:6
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