Protein aggregation in Escherichia coli: role of proteases. Export

@article{citeulike:1697516, abstract = {Protein aggregation is involved in several human diseases, and presumed to be an important process in protein quality control. In bacteria, aggregation of proteins occurs during stress conditions, such as heat shock. We studied the protein aggregates of Escherichia coli during heat shock. Our results demonstrate that the concentration and diversity of proteins in the aggregates depend on the availability of proteases. Aggregates obtained from mutants in the Lon (La) protease contain three times more protein than wild-type aggregates and show the broadest protein diversity. The results support the assumption that protein aggregates are formed from partially unfolded proteins that were not refolded by chaperones or degraded by proteases.}, address = {Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv, Tel Aviv 69978, Israel.}, author = {Rosen, R. and Biran, D. and Gur, E. and Becher, D. and Hecker, M. and Ron, E. Z.}, citeulike-article-id = {1697516}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/11886743}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=11886743}, day = {22}, issn = {0378-1097}, journal = {FEMS Microbiol Lett}, keywords = {aggregation, newtrp, proteases, protein}, month = {January}, number = {1}, pages = {9--12}, posted-at = {2007-09-26 16:00:27}, priority = {2}, title = {Protein aggregation in Escherichia coli: role of proteases.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/11886743}, volume = {207}, year = {2002} }

TY - JOUR ID - citeulike:1697516 L3 - citeulike-article-id:1697516 N2 - Protein aggregation is involved in several human diseases, and presumed to be an important process in protein quality control. In bacteria, aggregation of proteins occurs during stress conditions, such as heat shock. We studied the protein aggregates of Escherichia coli during heat shock. Our results demonstrate that the concentration and diversity of proteins in the aggregates depend on the availability of proteases. Aggregates obtained from mutants in the Lon (La) protease contain three times more protein than wild-type aggregates and show the broadest protein diversity. The results support the assumption that protein aggregates are formed from partially unfolded proteins that were not refolded by chaperones or degraded by proteases. IS - 1 JF - FEMS Microbiol Lett SN - 0378-1097 AD - Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv, Tel Aviv 69978, Israel. EP - 12 TI - Protein aggregation in Escherichia coli: role of proteases. VL - 207 SP - 9 KW - aggregation KW - newtrp KW - proteases KW - protein AU - Rosen, R AU - Biran, D AU - Gur, E AU - Becher, D AU - Hecker, M AU - Ron, EZ PY - 2002/01/22/ UR - http://view.ncbi.nlm.nih.gov/pubmed/11886743 ER -