Hemmingsen S M
Plant Biotechnology Institute, National Research Council Canada, Saskatoon, Saskatchewan.
Semin Cell Biol. 1990 Feb;1(1):47-54.
The discovery and properties of the plastid chaperonin are described. This chaperonin is implicated in the folding and assembly of the enzyme ribulose bisphosphate carboxylase-oxygenase and in the folding of proteins imported into plastids from the cytosol. The plastid chaperonin appears to be unique in that it contains two distinct types of 60 kDa polypeptide, whereas only a single subunit type has been reported for the bacterial and mitochondrial chaperonins. The plastid chaperonin polypeptides are encoded by nuclear genes which are subject to complex regulation.
本文描述了质体伴侣蛋白的发现及其特性。这种伴侣蛋白与核酮糖二磷酸羧化酶加氧酶的折叠和组装以及从细胞质导入质体的蛋白质的折叠有关。质体伴侣蛋白似乎很独特，因为它包含两种不同类型的60 kDa多肽，而细菌和线粒体伴侣蛋白仅报道有一种亚基类型。质体伴侣蛋白多肽由受复杂调控的核基因编码。
