伴随蛋白
莱茵衣藻
叶绿体
伴侣(临床)
蛋白酶
蛋白质亚单位
蛋白质折叠
质体
衣原体
蛋白酵素
蛋白质水解
细胞生物学
生物化学
低温电子显微
生物
生物物理学
化学
酶
突变体
病理
基因
医学
作者
Ning Wang,Yifan Wang,Qian Zhao,Xiang Zhang,Chao Peng,Wenjuan Zhang,Yanan Liu,Olivier Vallon,Michael Schroda,Yao Cong,Cuimin Liu
出处
期刊:Nature plants
[Springer Nature]
日期:2021-11-15
卷期号:7 (11): 1505-1515
被引量:8
标识
DOI:10.1038/s41477-021-01020-x
摘要
Protein homoeostasis 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 reinhardtii by cryo-electron microscopy. 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.
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