title: A nutrient uptake role for bacterial cell envelope extensions.
abstract: Bacteria exist in a variety of morphologies, but the relationship between cellular forms and biological functions remains poorly understood. We show that stalks (prosthecae), cylindrical extensions of the Caulobacter crescentus cell envelope, can take up and hydrolyze organic phosphate molecules and contain the high-affinity phosphate-binding protein PstS, but not PstA, a protein that is required for transport of phosphate into the cytoplasm. Therefore, uptake, hydrolysis, and periplasmic binding of a phosphate source can take place in the stalk, but high-affinity import must take place in the cell body. Furthermore, by using analytical modeling, we illustrate the biophysical advantage of the stalk as a morphological adaptation to the diffusion-limited, oligotrophic environments where C. crescentus thrives. This advantage is due to the fact that a stalk is long and thin, a favorable shape for maximizing contact with diffusing nutrients while minimizing increases in both surface area and cell volume.
authors.affiliation: Department of Biology, Indiana University, Bloomington, IN 47405, USA.
authors.forename: Jennifer K
authors.initials: JK
authors.lastname: Wagner
authors.forename: Sima
authors.initials: S
authors.lastname: Setayeshgar
authors.forename: Laura A
authors.initials: LA
authors.lastname: Sharon
authors.forename: James P
authors.initials: JP
authors.lastname: Reilly
authors.forename: Yves V
authors.initials: YV
authors.lastname: Brun
mesh_terms: D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism*; D001692:Biological Transport / Q000502:physiology; D016935:Caulobacter crescentus / Q000166:cytology / Q000378:metabolism; D048430:Cell Shape; D022081:Cell Surface Extensions / Q000378:metabolism* / Q000648:ultrastructure; D005456:Fluorescent Dyes / Q000378:metabolism; D033902:Periplasmic Binding Proteins / Q000378:metabolism; D028044:Phosphate-Binding Proteins / Q000378:metabolism; D010710:Phosphates / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D005456:Fluorescent Dyes; D033902:Periplasmic Binding Proteins; D028044:Phosphate-Binding Proteins; D010710:Phosphates