Polarized cells, polar actions.
The recognition of polar bacterial organization is just emerging. The examples of polar localization given here are from a variety of bacterial species and concern a disparate array of cellular functions. A number of well-characterized instances of polar localization of bacterial proteins, including the chemoreceptor complex in both C. crescentus and E. coli, the maltose-binding protein in E. coli, the B. japonicum surface attachment proteins, and the actin tail of L. monocytogenes within a mammalian cell, involve proteins or protein complexes that facilitate bacterial interaction with the environment, either the extracellular milieux or that within a plant or mammalian host. The significance of this observation remains unclear. Polarity in bacteria poses many problems, including the necessity for a mechanism for asymmetrically distributing proteins as well as a mechanism by which polar localization is maintained. Large structures, such as a flagellum, are anchored at the pole by means of the basal body that traverses the peptidoglycan wall. But for proteins and small complexes, whether in the periplasm or the membrane, one must invoke a mechanism that prevents the diffusion of these proteins away from the cell pole. Perhaps the periplasmic proteins are retained at the pole by the presence of the periseptal annulus (35). The constraining features for membrane components are not known. For large aggregates, such as the clusters of MCP, CheA, and CheW complexes, perhaps the size of the aggregate alone prevents displacement. In most cases of cellular asymmetry, bacteria are able to discriminate between the new pole and the old pole and to utilize this information for localization specificity. The maturation of new pole to old pole appears to be a common theme as well. Given numerous examples reported thus far, we propose that bacterial polarity displays specific rules and is a more general phenomenon than has been previously recognized.
Maddock
J R
JR
Department of Developmental Biology, Beckman Center, Stanford University School of Medicine, California 94305-5427.
Alley
M R
MR
Shapiro
L
L
D001419:Bacteria / Q000166:cytology; D018407:Bacterial Physiological Phenomena; D016935:Caulobacter crescentus / Q000166:cytology / Q000502:physiology; D002455:Cell Division; D004926:Escherichia coli / Q000166:cytology / Q000502:physiology; D008089:Listeria monocytogenes / Q000166:cytology / Q000502:physiology; D008954:Models, Biological; D012230:Rhizobiaceae / Q000166:cytology / Q000502:physiology; D012231:Rhizobium / Q000166:cytology / Q000502:physiology