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E. coli Transports Aggregated Proteins to the Poles by a Specific and Energy-Dependent Process
Authors:Assaf Rokney  Merav Shagan  Yoav Smith  Amos B. Oppenheim
Affiliation:1 Department of Microbiology and Molecular Genetics, IMRIC, Faculty of Medicine, The Hebrew University, POB. 12272, Ein Kerem, Jerusalem 91120, Israel
2 Laboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA
3 Genomic Data Analysis Unit, Hebrew University Medical School, Jerusalem 91120, Israel
Abstract:Aggregation of proteins due to failure of quality control mechanisms is deleterious to both eukaryotes and prokaryotes. We found that in Escherichia coli, protein aggregates are delivered to the pole and form a large polar aggregate (LPA). The formation of LPAs involves two steps: the formation of multiple small aggregates and the delivery of these aggregates to the pole to form an LPA. Formation of randomly distributed aggregates, their delivery to the poles, and LPA formation are all energy-dependent processes. The latter steps require the proton motive force, activities of the DnaK and DnaJ chaperones, and MreB. About 90 min after their formation, the LPAs are dissolved in a process that is dependent upon ClpB, DnaK, and energy. Our results confirm and substantiate the notion that the formation of LPAs allows asymmetric inheritance of the aggregated proteins to a small number of daughter cells, enabling their rapid elimination from most of the bacterial population. Moreover, the results show that the processing of aggregated proteins by the protein quality control system is a multi-step process with distinct spatial and temporal controls.
Keywords:LPA, large polar aggregate   PMF, proton motive force   HTS, homoserine trans-succinylase   GFP, green fluorescent protein   RDA, randomly distributed aggregate   CCCP, carbonyl cyanide m-chlorophenylhydrazone   OD600, optical density at 600   nm
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