Nature Plants
Abstract
Protein homeostasis in plastids is strategically regulated by the protein quality control system involving multiple chaperones and proteases, among them the Clp protease. Here we determined the structure of the chloroplast ClpP complex from Chlamydomonas reinhardtiiby cryo-EM. ClpP contains two heptameric catalytic rings without any symmetry. The top ring contains one ClpR6, three ClpP4 and three ClpP5 subunits while the bottom ring is composed of three ClpP1C subunits and one each of the ClpR1-4 subunits. ClpR3, ClpR4 and ClpT4 subunits connect the two rings and stabilize the complex. The chloroplast Cpn11/20/23 co-chaperonin, a co-factor of Cpn60, forms a cap on the top of ClpP by protruding mobile loops into hydrophobic clefts at the surface of the top ring. The co-chaperonin repressed ClpP proteolytic activity in vitro. By regulating Cpn60 chaperone and ClpP protease activity, the co-chaperonin may play a role in coordinating protein folding and degradation in the chloroplast.
| 论文编号: | DOI:10.1038/s41477-021-01020-x |
| 论文题目: | The Cryo-EM Structure of the Chloroplast ClpP Complex |
| 英文论文题目: | The Cryo-EM Structure of the Chloroplast ClpP Complex |
| 第一作者: | Ning Wang, Yifan Wang, Qian Zhao, Xiang Zhang, Chao Peng, Wenjuan Zhang, Yanan Liu, Olivier Vallon, Michael Schroda, Yao Cong, Cuimin Liu |
| 英文第一作者: | Ning Wang, Yifan Wang, Qian Zhao, Xiang Zhang, Chao Peng, Wenjuan Zhang, Yanan Liu, Olivier Vallon, Michael Schroda, Yao Cong, Cuimin Liu |
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| 发表年度: | 2021-11-16 |
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| 摘要: | Protein homeostasis in plastids is strategically regulated by the protein quality control system involving multiple chaperones and proteases, among them the Clp protease. Here we determined the structure of the chloroplast ClpP complex from Chlamydomonas reinhardtiiby cryo-EM. ClpP contains two heptameric catalytic rings without any symmetry. The top ring contains one ClpR6, three ClpP4 and three ClpP5 subunits while the bottom ring is composed of three ClpP1C subunits and one each of the ClpR1-4 subunits. ClpR3, ClpR4 and ClpT4 subunits connect the two rings and stabilize the complex. The chloroplast Cpn11/20/23 co-chaperonin, a co-factor of Cpn60, forms a cap on the top of ClpP by protruding mobile loops into hydrophobic clefts at the surface of the top ring. The co-chaperonin repressed ClpP proteolytic activity in vitro. By regulating Cpn60 chaperone and ClpP protease activity, the co-chaperonin may play a role in coordinating protein folding and degradation in the chloroplast. |
| 英文摘要: | Protein homeostasis in plastids is strategically regulated by the protein quality control system involving multiple chaperones and proteases, among them the Clp protease. Here we determined the structure of the chloroplast ClpP complex from Chlamydomonas reinhardtiiby cryo-EM. ClpP contains two heptameric catalytic rings without any symmetry. The top ring contains one ClpR6, three ClpP4 and three ClpP5 subunits while the bottom ring is composed of three ClpP1C subunits and one each of the ClpR1-4 subunits. ClpR3, ClpR4 and ClpT4 subunits connect the two rings and stabilize the complex. The chloroplast Cpn11/20/23 co-chaperonin, a co-factor of Cpn60, forms a cap on the top of ClpP by protruding mobile loops into hydrophobic clefts at the surface of the top ring. The co-chaperonin repressed ClpP proteolytic activity in vitro. By regulating Cpn60 chaperone and ClpP protease activity, the co-chaperonin may play a role in coordinating protein folding and degradation in the chloroplast. |
| 刊物名称: | Nature Plants |
| 英文刊物名称: | Nature Plants |
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| 其它备注: | Ning Wang, Yifan Wang, Qian Zhao, Xiang Zhang, Chao Peng, Wenjuan Zhang, Yanan Liu, Olivier Vallon, Michael Schroda, Yao Cong, Cuimin Liu. The Cryo-EM Structure of the Chloroplast ClpP Complex. Nature Plants. DOI:10.1038/s41477-021-01020-x |
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