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    National Tsing Hua University Institutional Repository > 理學院 > 化學系 > 期刊論文 >  Three-dimensional solution structures of the chromodomains of cpSRP43

    Please use this identifier to cite or link to this item: http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/56334

    Title: Three-dimensional solution structures of the chromodomains of cpSRP43
    Authors: Sivaraja V;Kumar TKS;Leena PST;Chang AN;Vidya C;Goforth RL;Rajalingam D;Arvind K;Ye JL;Chou J;Henry R;Yu C
    教師: 余靖
    Date: 2005
    Publisher: American Society for Biochemistry and Molecular Biology
    Relation: JOURNAL OF BIOLOGICAL CHEMISTRY, American Society for Biochemistry and Molecular Biology, Volume 280, Issue 50, DEC 16 2005, Pages 41465-41471
    Abstract: Chloroplasts contain a unique signal recognition particle (cpSRP). Unlike the cytoplasmic forms, the cpSRP lacks RNA but contains a conserved 54-kDa GTPase and a novel 43-kDa subunit (cpSRP43). Recently, three functionally distinct chromodomains (CDs) have been identified in cpSRP43. In the present study, we report the three-dimensional solution structures of the three CDs (CD1, CD2, and CD3) using a variety of triple resonance NMR experiments. The structure of CD1 consists of a triple-stranded beta-sheet segment. The C-terminal helical segment typically found in the nuclear chromodomains is absent in CD1. The secondary structural elements in CD2 and CD3 include a triple-stranded antiparallel beta-sheet and a C-terminal helix. Interestingly, the orientation of the C-terminal helix is significantly different in the structures of CD2 and CD3. Critical comparison of the structures of the chromodomains of cpSRP43 with those found in nuclear chromodomain proteins revealed that the diverse protein-protein interactions mediated by the CDs appear to stem from the differences that exist in the surface charge potentials of each CD. Results of isothermal titration calorimetry experiments confirmed that only CD2 is involved in binding to cpSRP54. The negatively charged C-terminal helix in CD2 possibly plays a crucial role in the cpSRP54-cpSRP43 interaction.
    URI: http://www.asbmb.org/
    Appears in Collections:[化學系] 期刊論文

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