TAILIEUCHUNG - Báo cáo khóa học: Identification of domains on the extrinsic 23 kDa protein possibly involved in electrostatic interaction with the extrinsic 33 kDa protein in spinach photosystem II

To elucidate the domains on the extrinsic 23 kDa protein involved inelectrostatic interactionwiththeextrinsic33 kDa protein in spinach photosystem II, we modified amino or carboxyl groups ofthe 23 kDa protein to unchargedmethyl ester groups with N-succinimidyl propionate or glycine methyl ester in the presence ofa water-soluble carbodi-imide, propionate-modified 23 kDa protein did not bind to the 33 kDa protein associ-atedwithPSIImembranes, whereas the glycinemethyl ester-modified 23 kDa protein completely bound. . | Eur. J. Biochem. 271 962-971 2004 FEBS 2004 doi Identification of domains on the extrinsic 23 kDa protein possibly involved in electrostatic interaction with the extrinsic 33 kDa protein in spinach photosystem II Akihiko Tohri1 2 Naoshi Dohmae3 Takehiro Suzuki1 Hisataka Ohta1 4. Yasunori Inoue2 4 and Isao Enami1 1 Department of Biology Faculty of Science Tokyo University of Science Kagurazaka Shinjuku-ku Tokyo Japan department of Applied Biological Science Faculty of Science and Technology Tokyo University of Science Yamazaki Noda Chiba Japan 3Division of Biochemical Characterization the Institute of Physical and Chemical Research RIKEN Hirosawa Wako Saitama Japan 4Tissue Engineering Research Center Tokyo University of Science Yamazaki Noda Chiba Japan To elucidate the domains on the extrinsic 23 kDa protein involved in electrostatic interaction with the extrinsic 33 kDa protein in spinach photosystem II we modified amino or carboxyl groups of the 23 11 Da prolei n to LI ndi a rged methyl ester groups with N-succinimidyl propionate or glycine methyl ester in the presence of a Wlller-roluhte caroodi-imide respectively. The N-succinimidyl propionate-modified 23 kDa protein did not bind to the 33 kDa protein associated with PSII membranes whereas the glycine methyl ester-modified 23 kDa protein completely bound. This indicates that positive charges on the 23 kDa protein are important for electrostatic interaction with the 33 kDa protein associated with the PSII membranes. Mapping of the N-succinimidyl propionate-modified sites ofthe 23 kDa protein was performed using Staphylococcus V8 protease digestion of the modified protein followed by determination of the mass of the resultant peptide fragments with MALDI-TOF MS. The results showed that six domains Lys11-Lys14 Lys27-Lys38 Lys40 Lys90-Lys96 Lys143-Lys152 Lys166-Lys174 were modified with N-sunninrmidyl propionate. In these domains Lys11 Lys13 Lys33 Lys38 Lys143 Lys166 Lys170 and .

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