Physics, Simon Fraser University, Burnaby, British Columbia, Canada.
PLoS Comput Biol. 2010 Nov 11;6(11):e1000986. doi: 10.1371/journal.pcbi.1000986.
The spatial patterning of proteins in bacteria plays an important role in many processes, from cell division to chemotaxis. In the asymmetrically dividing bacteria Caulobacter crescentus, a scaffolding protein, PopZ, localizes to both poles and aids the differential patterning of proteins between mother and daughter cells during division. Polar patterning of misfolded proteins in Escherichia coli has also been shown, and likely plays an important role in cellular ageing. Recent experiments on both of the above systems suggest that the presence of chromosome free regions along with protein multimerization may be a mechanism for driving the polar localization of proteins. We have developed a simple physical model for protein localization using only these two driving mechanisms. Our model reproduces all the observed patterns of PopZ and misfolded protein localization--from diffuse, unipolar, and bipolar patterns and can also account for the observed patterns in a variety of mutants. The model also suggests new experiments to further test the role of the chromosome in driving protein patterning, and whether such a mechanism is responsible for helping to drive the differentiation of the cell poles.
蛋白质在细菌中的空间模式在许多过程中起着重要作用,从细胞分裂到趋化性。在不对称分裂的细菌新月柄杆菌中,支架蛋白 PopZ 定位于两极,并有助于在分裂过程中母细胞和子细胞之间对蛋白质进行差异模式化。在大肠杆菌中也观察到了错误折叠蛋白质的极性模式化,并且可能在细胞衰老中起重要作用。最近对上述两个系统的实验表明,染色体无区域的存在以及蛋白质多聚化可能是驱动蛋白质极性定位的一种机制。我们仅使用这两种驱动机制开发了一种用于蛋白质定位的简单物理模型。我们的模型再现了 PopZ 和错误折叠蛋白定位的所有观察到的模式——从弥散的、单极的和双极的模式,并且还可以解释各种突变体中的观察到的模式。该模型还提出了新的实验来进一步测试染色体在驱动蛋白质模式化中的作用,以及这种机制是否有助于推动细胞两极的分化。