Created by gina_evans0312
about 11 years ago
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Question | Answer |
Types of Heat Shock Proteins in Prokaryotes | Cytoplasmic & Periplasmic |
Types of Heat Shock Proteins in Eukaryotes | Cytoplasmic, Nuclear, ER & Perinuclear |
HSP Size range | 14-40 kDa |
HSP reguation | Phosphorylation |
Normal Role of Hsp27 | Stabilisation of actin |
Phosphorylation of Hsp27 | Decreases size of oligomers- keeps it in small, probably dimeric form |
Hsp27 in cell under stress | Are dephosphorylated and form mutimers (700-800kDa) |
Role of Hsp27 in cell under stress | Binds to unfolded protein to store for refolding |
Structure of Hsp16.9 | Dodedecamer- 2 layers of 6 monomers |
Dimensions of Hsp16.9 | 120x65A |
Role of HSP's | Bind to unfolding proteins and stabilise them for refolding later |
Immunoglobulin Domain | |
Structure of Ig domain | 2 layers of aligned beta sheets (6-9 stands each) with a Greek key motif |
Dimerisation of Ig domain | Allows dimerisation of Hsp's |
What is PapD? | A bacterial homologue of Hsp's |
Location of PapD | Periplasmic Space |
Role of PapD | Pilus Construction |
Prevention of Innapropriate Pap_ Interactions | Pap F, E, K, A, H, G don't have a complex Ig domain, which must be completed by PapD's |
Chaperone Donor Strand Complimentation in Pap Proteins | PapD donates a beta sheet to the others to complete their Ig folds, allowing them to react only when they're supposed to |
Site of PapD donation | Missing bets strand forms a groove of sites P2-5- PapD's beta binds to P2-5 |
Nte | Contained by all Pap proteins but PapG & allows Pap proteins to bind together |
Donor Strand Exchange | |
Role of P5 Residue/Pocket | With PapD bound, P5 of incoming Pap protein binds to P5 pocket of PapD bound protein |
Once Donor Strand Complimentation is complete | The binding Pap protein competes out PapD and binds to the other Pap protein using it's Nte domain |
Pap protein competitiveness | The sequence of Pap proteins determines their affinity for others, which determines where in the Pili sequence they go |
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