Downregulation of rubisco activity by non-enzymatic acetylation of rbcl
文献类型:期刊论文
作者 | Gao, Xiang1,4; Hong, Hui1,4; Li, Wei-Chao3,4; Yang, Lili2,4; Huang, Jirong1,2; Xiao, You-Li3; Chen, Xiao-Ya1; Chen, Gen-Yun2 |
刊名 | Molecular plant
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出版日期 | 2016-07-06 |
卷号 | 9期号:7页码:1018-1027 |
关键词 | Rubisco Lysine acetylation Lys201 Lys334 4-methylumbelliferone esters |
ISSN号 | 1674-2052 |
DOI | 10.1016/j.molp.2016.03.012 |
通讯作者 | Chen, xiao-ya(xychen@sibs.ac.cn) ; Chen, gen-yun(chenggy@sibs.ac.cn) |
英文摘要 | Atmospheric carbon dioxide (co2) is assimilated by the most abundant but sluggish enzyme, ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco). here we show that acetylation of lysine residues of the rubisco large subunit (rbcl), including lys201 and lys334 in the active sites, may be an important mechanism in the regulation of rubisco activities. it is well known that lys201 reacts with co2 for carbamylation, a prerequisite for both carboxylase and oxygenase activities of rubisco, and lys334 contacts with ribulose-1,5-bisphosphate (rubp). the acetylation level of rbcl in plants is lower during the day and higher at night, inversely correlating with the rubisco carboxylation activity. a search of the chloroplast proteome database did not reveal a canonical acetyltransferase; instead, we found that a plant-derived metabolite, 7-acetoxy-4-methylcoumarin (amc), can non-enzymatically acetylate both native rubisco and synthesized rbcl peptides spanning lys334 or lys201. furthermore, lysine residues were modified by synthesized 4-methylumbelliferone esters with different electro- nd stereo-substitutes, resulting in varied rubisco activities. 1-chloroethyl 4-methylcoumarin-7-yl carbonate (clmc) could transfer the chloroethyl carbamate group to lysine residues of rbcl and completely inactivate rubisco, whereas bis(4-methylcoumarin-7-yl) carbonate (bmc) improved rubisco activity through increasing the level of lys201 carbamylation. our findings indicate that rbcl acetylation negatively regulates rubisco activity, and metabolic derivatives can be designed to dissect and improve co2 fixation efficiency of plants through lysine modification. |
WOS关键词 | ARABIDOPSIS-THALIANA ; LYSINE ACETYLATION ; HEXADECAMERIC RUBISCO ; CRYSTAL-STRUCTURE ; PROTEIN ; CARBOXYLASE ; ACTIVASE ; MEMBRANE ; ENZYMES ; WIDESPREAD |
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:000379655800007 |
出版者 | CELL PRESS |
URI标识 | http://www.irgrid.ac.cn/handle/1471x/2374664 |
专题 | 中国科学院大学 |
通讯作者 | Chen, Xiao-Ya; Chen, Gen-Yun |
作者单位 | 1.CAS Ctr Excellence Mol Plant Sci, State Key Lab Plant Mol Genet, Shanghai 200032, Peoples R China 2.Shanghai Inst Biol Sci, Lab Photosynth & Environm Biol, Shanghai 200032, Peoples R China 3.Shanghai Inst Biol Sci, Inst Plant Physiol & Ecol, CAS Lab Synthet Biol, Shanghai 200032, Peoples R China 4.Univ Chinese Acad Sci, Shanghai 200032, Peoples R China |
推荐引用方式 GB/T 7714 | Gao, Xiang,Hong, Hui,Li, Wei-Chao,et al. Downregulation of rubisco activity by non-enzymatic acetylation of rbcl[J]. Molecular plant,2016,9(7):1018-1027. |
APA | Gao, Xiang.,Hong, Hui.,Li, Wei-Chao.,Yang, Lili.,Huang, Jirong.,...&Chen, Gen-Yun.(2016).Downregulation of rubisco activity by non-enzymatic acetylation of rbcl.Molecular plant,9(7),1018-1027. |
MLA | Gao, Xiang,et al."Downregulation of rubisco activity by non-enzymatic acetylation of rbcl".Molecular plant 9.7(2016):1018-1027. |
入库方式: iSwitch采集
来源:中国科学院大学
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