Viollier Patrick H, Sternheim Nitzan, Shapiro Lucy
Department of Developmental Biology, Beckman Center, B351, 279 Campus Drive, Stanford University School of Medicine, Palo Alto, CA 94305-5329, USA.
EMBO J. 2002 Sep 2;21(17):4420-8. doi: 10.1093/emboj/cdf454.
Each cell division in Caulobacter crescentus is asymmetric, yielding a swarmer cell with several polar pili and a non-piliated stalked cell. To identify factors contributing to the asymmetric biogenesis of polar pili, cytological studies of pilus assembly components were performed. We show here that the CpaC protein, which is thought to form the outer membrane pilus secretion channel, and its assembly factor, CpaE, are localized to the cell pole prior to the polymerization of the pilus filament. We demonstrate that the PleC histidine kinase, a two-component signal transduction protein shown previously to localize to the piliated cell pole before and during pilus assembly, controls the accumulation of the pilin subunit, PilA. Using an inactive form of PleC (PleCH610A) that lacks the catalytic histidine residue, we provide evidence that PleC activity is responsible for the asymmetric distribution of CpaE and itself to only one of the two cell poles. Thus, a polar signal transduction protein controls its own asymmetric location as well as that of a factor assembling a polar organelle.
新月柄杆菌的每次细胞分裂都是不对称的,产生一个带有几根极毛的游动细胞和一个无纤毛的柄细胞。为了确定导致极毛不对称生物合成的因素,我们对菌毛组装成分进行了细胞学研究。我们在此表明,被认为形成外膜菌毛分泌通道的CpaC蛋白及其组装因子CpaE,在菌毛丝聚合之前就定位于细胞极。我们证明,PleC组氨酸激酶是一种双组分信号转导蛋白,先前已证明在菌毛组装之前和期间定位于有纤毛的细胞极,它控制菌毛蛋白亚基PilA的积累。使用缺乏催化组氨酸残基的无活性形式的PleC(PleCH610A),我们提供了证据表明PleC活性负责CpaE及其自身仅向两个细胞极之一的不对称分布。因此,一种极性信号转导蛋白控制其自身的不对称定位以及组装极性细胞器的因子的定位。