Coordinate synthesis and turnover of heat shock proteins in Borrelia burgdorferi: degradation of DnaK during recovery from heat shock.

摘要: The synthesis and turnover of heat shock proteins (Hsps) by Borrelia burgdorferi, the Lyme disease spirochete, was investigated radiolabeling whole spirochetes spheroplasts, comparison one- two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis, use immunochemistry. approximately 72-kDa DnaK homolog three additional Hsps 39, 27, 21 kDa increased in amount 3- to 15-fold between 2 6 h following temperature upshift from 28 39 degrees C. Temperature downshift experiments transfer 40 C showed that within 15 30 min, most major returned levels seen statically maintained at lower temperature. Spheroplasts B. burgdorferi produced treatment with EDTA lysozyme were radiolabeled, specific localized either cytoplasm or membrane fraction. Further analysis electrophoresis demonstrated constitutively expressed isoforms pIs near 5.5. A pattern suggestive degradation observed recovery but not entirely a low Some these putative products recognized monoclonal antibodies directed against protein. These data suggest period peak synthesis, is actively degraded as spirochete reestablishes its metabolic thermometer. findings provide new interpretation previous work suggesting 10 polypeptides, including have common epitope.