Zipper-like interaction between proteins in adjacent daughter cells mediates protein localization

被引:88
作者
Blaylock, B
Jiang, X
Rubio, A
Moran, CP
Pogliano, K [1 ]
机构
[1] Univ Calif San Diego, Div Biol Sci, La Jolla, CA 92093 USA
[2] Emory Univ, Sch Med, Dept Microbiol & Immunol, Atlanta, GA 30322 USA
关键词
sporulation; protein localization; signal transduction; bacterial development;
D O I
10.1101/gad.1252704
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Protein localization is crucial for cellular morphogenesis and intracellular signal transduction cascades. Here we describe an interaction between two membrane proteins expressed in different cells of the Bacillus subtilis sporangium, the mother cell protein SpoIIIAH and the forespore protein SpoIIQ. We used affinity chromatography, coimmunoprecipitation, and the yeast two-hybrid system to demonstrate that the extracellular domains of these proteins interact, tethering SpoIIIAH to the sporulation septum, and directing its assembly with SpoIIQ into helical arcs and foci around the forespore. We also demonstrate that this interaction can direct proteins made in the same cell to active division sites, as when SpoIIQ is made in the mother cell, it localizes to nascent septa in a SpoIIIAH-dependent manner. Both SpoIIIAH and SpollQ are necessary for activation of the second forespore-specific transcription factor (sigma(G)) after engulfment, and we propose that the SpoIIIAH-SpoIIQ complex contributes to a morphological checkpoint coupling sigma(G) activation to engulfment. In keeping with this hypothesis, SpolIlAH localization depends on the first step of engulfment, septal thinning. The SpoIIQ-SpoIIIAH complex reaches from the mother cell cytoplasm to the forespore cytoplasm and is ideally positioned to govern the activity of engulfment-dependent transcription factors.
引用
收藏
页码:2916 / 2928
页数:13
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