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Positive Charges on Lysine Residues of the Extrinsic 18 kDa Protein Are Important to Its Electrostatic Interaction with Spinach Photosystem Ⅱ Membranes

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Acta Biochimica et Biophysica Sinica 2005年第11期37卷 737-742页

作者： jin-peng gao Zhen-Hua YONG feng zhang kang-cheng ruan chun-he xu Gen-Yun CheN institute of plant physiology & ecology.shanghai institutes for biological sciences,chinese Academy of sciences,shanghai 2.0032.china Laboratory of Proteomics,institute of Biochemistry and Cell Biology,shanghai institutes for biological sciences,chinese Academy of sciences,shanghai 200031,china College of sciences,Zhejiang University.Hangzhou 310029,china Graduate School of the chinese Academy of sciences,shanghai 2.0032.china institute of plant {2. & ecology Shanghai Institutes for Biological Sciences Chinese Academy of SciencesShanghai 200032 China Graduate School of the chinese Aca{2.my of sciencesshanghai 2.0032 China College of sciences Zhejiang UniversityHangzhou 310029 China Laboratory of Proteomics Institute of Biochemistry and Cell Biology Shanghai Institutes for Biological Sciences Chinese Academy of SciencesShanghai 200031 China

To determine the contribution of charged amino acids to binding with the photosystem Ⅱcomplex(PSⅡ),the amino or carboxyl groups of the extrinsic 18 kDa protein were modified with N-succinimidyl propionate(NSP)or glycine methyl ester(GME)in the presence of a water-soluble carbodiimide,*** on isoelectric point shift,4-10 and 10-14 amino groups were modified in the presence of2.and 4 mM NSP,***,3-4 carboxyl groups were modified by reaction with *** of negatively charged carboxyl groups with GME did not alter the binding activity of theextrinsic 18 kDa ***,the NSP-modified 18 kDa protein,in which the positively charged aminogroups had been modified to uncharged methyl esters,failed to bind with the PSⅡ membrane in the presenceof the extrinsic 2. kDa *** defect can not be attributed to structural or conformational alterationsimposed by chemical modification,as the fluorescence and circular dichroism spectra among native,GME-and NSP-modified extrinsic 18 kDa proteins were ***,we have concluded that the positive chargesof lysyl residues in the extrinsic 18 kDa protein are important for its interaction with PSⅡ membranes in thepresence of the extrinsic 2. kDa ***,it was found that the negative charges of carboxylgroups of this protein did not participate in binding with the extrinsic 2. kDa protein associated with PSⅡmembranes.

关键词： extrinsic 18 kDa protein circular dichroism electrostatic interaction chemical modification

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Six Specific Lysihe Residues are Crucial in Maintaining the Structure and Function of Soluble Manganese Stabi{2.zing Protein

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Acta Biochimica et Biophysica Sinica 2006年第9期 611-619页

作者： jin-peng gao~(1,2#) feng zhang~(1,3#) li zhang~4 yin-long guo~4 kang-cheng ruan~5 de-An jiang~3* chun-he xu~1 1 institute of plant physiology and ecology,shanghai institutes for biological sciences,chinese Academy of sciences,shanghai 2.0032.china 2 Graduate School of the chinese Academy of sciences,shanghai 2.0032.china 3 College of life sciences,Zhejiang University,Hangzhou 310029,china 4 shanghai Mass Spectrometry Center,shanghai institute of Organic Chemistry,chinese Academy of sciences,shanghai 200031,china 5 Laboratory of Proteomics,institute of Biochemistry and Cell Biology,shanghai institutes for biological sciences,chinese Academy of sciences,shanghai 200031,china

When manganese stabilizing protein （MSP） was treated with 0.5mM N-succinimidyl propionate（NSP）,the rebinding ability and oxygen-releasing capabilities of the modified MSP were not altered,in spiteof changes of MSP surface Lys ***,far-ultraviolet circular dichroism and intrinsicfluorescence spectra analysis revealed that 0.5 mM NSP-modified MSP retained most of its native secondaryand tertiary *** of the sites of NSP modification by Staphylococcus V8protease digestion ofthe modified protein,as well as analysis by matrix-assisted laser desorption ionization-time of flight massspectrometry,indicated that seven Lys residues were *** results suggested that these residues arenot absolutely essential to the structure and function of ***,when the NSP concentration wasincreased to 4mM,the modified MSP was unable to bind photosystem Ⅱ and completely lost its *** far-ultraviolet circular dichroism and intrinsic fluorescence spectra analysis revealed a clearconformational change in MSP after 4 mM NSP treatment,suggesting that some Lys residues are involved inmaintaining the structure and function of *** by matrix-assisted laser desorption ionization-timeof flight mass spectrometry indicated that another six Lys residues,namely Lys2.,Lys101,Lys196,Lys2.7,Lys130 （or Lys137） and Lys66 （or Lys76）,were modified by 4 mM ***,these six Lys residuesare crucial in maintaining the structure and function of soluble MSP.

关键词： chemical modification fluorescence spectrum circular dichroism spectrum manganese stabilizing protein Lys residue

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