A nutrient uptake role for bacterial cell envelope extensions
- 1 August 2006
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 103 (31) , 11772-11777
- https://doi.org/10.1073/pnas.0602047103
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.Keywords
This publication has 68 references indexed in Scilit:
- De novo backbone scaffolds for protein designProteins-Structure Function and Bioinformatics, 2009
- PEP-FOLD: an online resource for de novo peptide structure predictionNucleic Acids Research, 2009
- Structural Alphabets for Protein Structure Classification: A Comparison StudyJournal of Molecular Biology, 2009
- PiSite: a database of protein interaction sites using multiple binding states in the PDBNucleic Acids Research, 2008
- Protein sequence and structure alignments within one frameworkAlgorithms for Molecular Biology, 2008
- SEQOPTICS: a protein sequence clustering systemBMC Bioinformatics, 2006
- SABBAC: online Structural Alphabet-based protein BackBone reconstruction from Alpha-Carbon traceNucleic Acids Research, 2006
- GROMACS: Fast, flexible, and freeJournal of Computational Chemistry, 2005
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- THE FINE STRUCTURE OF STALKED BACTERIA BELONGING TO THE FAMILY CAULOBACTERACEAEThe Journal of cell biology, 1964