Essential Role of the Cytoplasmic Chemoreceptor TlpT in the Formation of Chemosensory Complexes in Rhodobacter sphaeroides.

Bacterial chemosensory proteins form large hexagonal arrays. Several key features of chemotactic signaling depend on these large arrays, namely, cooperativity between receptors, sensitivity, integration of different signals, and adaptation. The best-studied arrays are the membrane-associated arrays found in most bacteria. has two spatially distinct chemosensory arrays, one is transmembrane and the other is cytoplasmic. These two arrays work together to control a single flagellum. Deletion of one of the soluble chemoreceptors, TlpT, results in the loss of the formation of the cytoplasmic array. Here, we show the expression of TlpT in a deletion background results in the reformation of the cytoplasmic array. The number of arrays formed is dependent on the cell length, indicating spatial limitations on the number of arrays in a cell and stochastic assembly. Deletion of PpfA, a protein required for the positioning and segregation of the cytoplasmic array, results in slower array formation upon TlpT expression and fewer arrays, suggesting it accelerates cluster assembly. Bacterial chemosensory arrays are usually membrane associated and consist of thousands of copies of receptors, adaptor proteins, kinases, and adaptation enzymes packed into large hexagonal structures. also has cytoplasmic arrays, which divide and segregate using a chromosome-associated ATPase, PpfA. The expression of the soluble chemoreceptor TlpT is shown to drive the formation of the arrays, accelerated by PpfA. The positioning of these arrays suggests their position is the result of stochastic assembly rather than active positioning.