Activity of the Hsp70 chaperone complex--DnaK, DnaJ, and GrpE--in initiating phage lambda DNA replication by sequestering and releasing lambda P protein
| Autor: | Harrison Echols, Marie-Agnès Petit, Chi Lu, Heidi J. Hoffmann, Susan K. Lyman |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
DNA Replication
Chaperonins Macromolecular Substances Virus Replication Origin of replication Viral Proteins Bacterial Proteins Heat shock protein Escherichia coli HSP70 Heat-Shock Proteins Heat-Shock Proteins dnaB helicase Multidisciplinary biology Escherichia coli Proteins DNA Helicases DNA replication Proteins HSP40 Heat-Shock Proteins Lambda phage biology.organism_classification Bacteriophage lambda Molecular biology DNA-Binding Proteins Chaperone (protein) DNA Viral biology.protein Biophysics bacteria Chaperone complex Protein folding DnaB Helicases Protein Binding Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 89:12108-12111 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.89.24.12108 |
| Popis: | Initiation of DNA replication by phage lambda requires the ordered assembly and disassembly of a specialized nucleoprotein structure at the origin of replication. In the disassembly pathway, a set of Escherichia coli heat shock proteins termed the Hsp70 complex--DnaK, DnaJ, and GrpE--act with ATP to release lambda P protein from the nucleo-protein complex, freeing the DnaB helicase for its DNA-unwinding reaction. To investigate the mechanism of the release reaction, we have examined the interaction between P and the three heat shock proteins by glycerol gradient sedimentation and gel electrophoresis. We have discovered an ATP-dependent ternary interaction between P, DnaK, and DnaJ; this P.DnaK.DnaJ complex is dissociated by GrpE. We have concluded that the function of the Hsp70 complex in sequestering and releasing P protein provides for the critical step in the disassembly pathway. Based on our data and other work on protein folding, the formation of the P.DnaK.DnaJ complex might involve a conformational shift to a folding intermediate of P. |
| Databáze: | OpenAIRE |
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