Six specific lysine residues are crucial in maintaining the structure and function of soluble manganese stabilizing protein
文献类型：期刊论文
| 作者 | Gao, JP; Zhang, F; Zhang, L; Guo, YL; Ruan, KC; Jiang, DA; Xu, CH |
| 刊名 | ACTA BIOCHIMICA ET BIOPHYSICA SINICA
 |
| 出版日期 | 2006 |
| 卷号 | 38期号:9页码:611-619 |
| 关键词 | chemical modification fluorescence spectrum circular dichroism spectrum manganese stabilizing protein Lys residue |
| 通讯作者 | Jiang, DA (reprint author), Chinese Acad Sci, Inst Plant Physiol & Ecol, Shanghai Inst Biol Sci, 345 Lingling Lu, Shanghai 200032, Peoples R China.,dajiang@zju.edu.cn ; xch@sippe.ac.cn |
| 英文摘要 | When manganese stabilizing protein (MSP) was treated with 0.5 mM N-succinimidyl propionate (NSP), the rebinding ability and oxygen-releasing capabilities of the modified MSP were not altered, in spite of changes of MSP surface Lys residues. Furthermore, far-ultraviolet circular dichroism and intrinsic fluorescence spectra analysis revealed that 0.5 mM NSP-modified MSP retained most of its native secondary and tertiary structure. Mapping of the sites of NSP modification by Staphylococcus V-8 protease digestion of the modified protein, as well as analysis by matrix-assisted laser desorption ionization-time of flight mass spectrometry, indicated that seven Lys residues were modified. The results suggested that these residues are not absolutely essential to the structure and function of MSP. However, when the NSP concentration was increased to 4 mM, the modified MSP was unable to bind photosystem II and completely lost its reactivating capability. Both far-ultraviolet circular dichroism and intrinsic fluorescence spectra analysis revealed a clear conformational change in MSP after 4 mM NSP treatment, suggesting that some Lys residues are involved in maintaining the structure and function of MSP. Analysis by matrix-assisted laser desorption ionization-time of flight mass spectrometry indicated that another six Lys residues, namely Lys20, Lys101, Lys196, Lys207, Lys130 (or Lys137) and Lys66 (or Lys76), were modified by 4 mM NSP. Therefore, these six Lys residues are crucial in maintaining the structure and function of soluble MSP. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 关键词[WOS] | PHOTOSYNTHETIC OXYGEN-EVOLUTION ; 33-KDA EXTRINSIC PROTEIN ; SPINACH PHOTOSYSTEM-II ; ELECTROSTATIC INTERACTION ; 33-KILODALTON PROTEIN ; KDA PROTEIN ; RECONSTITUTION ; POLYPEPTIDE ; IDENTIFICATION ; CHLOROPLASTS |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000240524100003 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/1757]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Gao, JP,Zhang, F,Zhang, L,et al. Six specific lysine residues are crucial in maintaining the structure and function of soluble manganese stabilizing protein[J]. ACTA BIOCHIMICA ET BIOPHYSICA SINICA,2006,38(9):611-619. |
| APA | Gao, JP.,Zhang, F.,Zhang, L.,Guo, YL.,Ruan, KC.,...&Xu, CH.(2006).Six specific lysine residues are crucial in maintaining the structure and function of soluble manganese stabilizing protein.ACTA BIOCHIMICA ET BIOPHYSICA SINICA,38(9),611-619. |
| MLA | Gao, JP,et al."Six specific lysine residues are crucial in maintaining the structure and function of soluble manganese stabilizing protein".ACTA BIOCHIMICA ET BIOPHYSICA SINICA 38.9(2006):611-619. |
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