Mutation of residue arginine(18) of cytochrome b(559) alpha-subunit and its effects on photosystem ii activities in chlamydomonas reinhardtii
文献类型：期刊论文
| 作者 | Ma, Jing-Jing; Li, Liang-Bi; Jing, Yu-Xiang; Kuang, Ting-Yun |
| 刊名 | Journal of integrative plant biology
 |
| 出版日期 | 2007-07-01 |
| 卷号 | 49期号:7页码:1054-1061 |
| 关键词 | Chlamydomonas reinhardtii Chloroplast transformation Cytochrome b(559) Mutation Photosystem ii |
| ISSN号 | 1672-9072 |
| DOI | 10.1111/j.1672-9072.2007.00486.x |
| 通讯作者 | Kuang, ting-yun(kuangty@ibcas.ac.cn) |
| 英文摘要 | It has been known that arginine is used as the basic amino acid in the alpha-subunit of cytochrome b(559) (cyt b(559)) except histidine. however, previous studies have focused on the function of histidine in the activities of photosystem (ps) ii and there are no reports regarding the structural and/or functional roles of arginine in psii complexes. in the present study, two arginine(18) (r18) mutants of chlamydomonas reinhardtii were constructed using site-directed mutagenesis, in which r18 was replaced by glutamic acid (e) and glycine (g). the results show that the oxygen evolution of the psii complex in the r18g and r18e mutants was approximately 60% of wild-type (wt) levels and that, after irradiation at high light intensity, oxygen evolution for the psii of mutants was reduced to zero compared with 40% in wt cells. the efficiency of light capture by psii (f-v/f-m) of r18g and r18e mutants was approximately 42%-46% that of wt cells. furthermore, levels of the alpha-subunit of cyt b(559) and psbo proteins were reduced in thylakoid membranes compared with wt. overall, these data suggest that r18 plays a significant role in helping cyt b(559) maintain the structure of the psii complex and its activity, although it is not directly bound to the heme group. |
| WOS关键词 | SITE-DIRECTED MUTAGENESIS ; AXIAL LIGANDS ; PSBF GENES ; CHLOROPLAST ; B(559) ; PHOTOSYNTHESIS ; B-559 ; DARK ; TRANSFORMATION ; PLASTOQUINONE |
| WOS研究方向 | Biochemistry & Molecular Biology ; Plant Sciences |
| WOS类目 | Biochemistry & Molecular Biology ; Plant Sciences |
| 语种 | 英语 |
| WOS记录号 | WOS:000247442100011 |
| 出版者 | BLACKWELL PUBLISHING |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2381611 |
| 专题 | 中国科学院大学 |
| 通讯作者 | Kuang, Ting-Yun |
| 作者单位 | 1.Chinese Acad Sci, Inst Bot, Key Lab Photosynth & Environm Mol Physiol, Beijing 100093, Peoples R China 2.Grad Univ, Chinese Acad Sci, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Ma, Jing-Jing,Li, Liang-Bi,Jing, Yu-Xiang,et al. Mutation of residue arginine(18) of cytochrome b(559) alpha-subunit and its effects on photosystem ii activities in chlamydomonas reinhardtii[J]. Journal of integrative plant biology,2007,49(7):1054-1061. |
| APA | Ma, Jing-Jing,Li, Liang-Bi,Jing, Yu-Xiang,&Kuang, Ting-Yun.(2007).Mutation of residue arginine(18) of cytochrome b(559) alpha-subunit and its effects on photosystem ii activities in chlamydomonas reinhardtii.Journal of integrative plant biology,49(7),1054-1061. |
| MLA | Ma, Jing-Jing,et al."Mutation of residue arginine(18) of cytochrome b(559) alpha-subunit and its effects on photosystem ii activities in chlamydomonas reinhardtii".Journal of integrative plant biology 49.7(2007):1054-1061. |
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来源：中国科学院大学
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