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Created by gina_evans0312
almost 12 years ago
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| Question | Answer |
| Size of Cytoplasmic Dyenin | 350 kDa |
| Dyenin Superfamily | AAA+ |
| Direction of C.Dyenin movement | From plus end to minus end |
| Cargo | mRNA, proteins, viruses- it varies |
| Role of Multiple Light Chain | Where cargo binds |
| No of heavy chains | 2 |
| AAA+ domains | Form a hexameric motor domain |
| Role of Linker domain | Dimerises protein |
| Coiled coil | Links AAA+ motor heads to microtubule binding site |
| N-terminus | Light chains, dimerisation and cargo binding |
| C terminus | AAA+ motors, tubulin binding and linking coiled coil stalk |
| Location of ATP binding | AAA+ domains |
| Binding of ATP changes | Relative positions of linker domains and coiled coil |
| ATP binding causes _ of MTBD | Weakening of MTBD to tubulin |
| No of ATP req'd | Unclear |
| Distance moved by Dyenin heads | 16nm- but it varies a lot |
| Largest known 'step' of head | 30 nm |
| Backwards movement | Possible |
| Movement onto other microtubules | Allows it to pass kinesin (kinesin can't change M.T's) |
| Mutant with non-functioning ATP head | Still moved, but slowly and with no powerstroke |
| Co-ordination of Dyenin movement | Much less co-ordinated than kinesin |
| Mechanism of movement | Hand over Hand model |
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