Functional analysis of the protein-interacting domains of chloroplast SRP43.
作者： Esther Jonas-Straube , Claire Hutin , Neil E. Hoffman , Danja Schünemann
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摘要: The chloroplast signal recognition particle (cpSRP) consists of an evolutionarily conserved 54-kDa subunit (cpSRP54) and a dimer unique 43-kDa (cpSRP43). cpSRP binds light-harvesting chlorophyll proteins (LHCPs) to form cpSRP/LHCP transit complex, which targets LHCP the thylakoid membrane. Previous studies showed that complex formation is mediated through binding L18 domain cpSRP43. cpSRP43 characterized by four-ankyrin repeat at N terminus two chromodomains C terminus. In present study we used yeast two-hybrid system in vitro assays analyze function different domains protein formation. We report here first ankyrin 18-amino acid on cpSRP43, whereas third fourth repeats are involved dimerization show further interaction with cpSRP54 via methionine-rich C-terminally located Both contain essential elements for cpSRP54, indicating closely spaced together create single site cpSRP54. addition, our data demonstrate enhanced indirectly motif
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