Created by gina_evans0312
almost 11 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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