@article{84361,
  keywords = {Escherichia coli, Microscopy, Phase-Contrast, Escherichia coli Proteins, Fluorescence Recovery After Photobleaching, Peptidoglycan, Bacterial Outer Membrane Proteins, Inclusion Bodies, N-Acetylglucosaminyltransferases, Phospholipids},
  author = {Allison Michaelis and Zemer Gitai},
  title = {Dynamic polar sequestration of excess MurG may regulate enzymatic function.},
  abstract = {<p>Advances in bacterial cell biology have demonstrated the importance of protein localization for protein function. In general, proteins are thought to localize to the sites where they are active. Here we demonstrate that in Escherichia coli, MurG, the enzyme that mediates the last step in peptidoglycan subunit biosynthesis, becomes polarly localized when expressed at high cellular concentrations. MurG only becomes polarly localized at levels that saturate MurG{\textquoteright}s cellular requirement for growth, and E. coli cells do not insert peptidoglycan at the cell poles, indicating that the polar MurG is not active. Fluorescence recovery after photobleaching (FRAP) and single-cell biochemistry experiments demonstrate that polar MurG is dynamic. Polar MurG foci are distinct from inclusion body aggregates, and polar MurG can be remobilized when MurG levels drop. These results suggest that polar MurG represents a temporary storage mechanism for excess protein that can later be remobilized into the active pool. We investigated and ruled out several candidate pathways for polar MurG localization, including peptidoglycan biosynthesis, the MreB cytoskeleton, and polar cardiolipin, as well as MurG enzymatic activity and lipid binding, suggesting that polar MurG is localized by a novel mechanism. Together, our results imply that inactive MurG is dynamically sequestered at the cell poles and that prokaryotes can thus utilize subcellular localization as a mechanism for negatively regulating enzymatic activity.</p>
},
  year = {2010},
  journal = {J Bacteriol},
  volume = {192},
  pages = {4597-605},
  month = {09/2010},
  issn = {1098-5530},
  doi = {10.1128/JB.00676-10},
  language = {eng},
}