E. coli Transports Aggregated Proteins to the Poles by a Specific and Energy-Dependent Process |
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Authors: | Assaf Rokney Merav Shagan Yoav Smith Amos B. Oppenheim |
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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 |
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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. |
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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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