Adamska I, Kloppstech K
Institut für Botanik, Universität Hannover, Federal Republic of Germany.
Eur J Biochem. 1991 Jun 1;198(2):375-81. doi: 10.1111/j.1432-1033.1991.tb16025.x.
The precursor to the nuclear-coded 22-kDa heat-shock protein of chloroplasts (HSP 22) has been transported into isolated intact chloroplasts from heat-shocked plants. The localization of the mature protein in the chloroplast membrane was investigated. We have shown that the processed HSP 22 of pea was not bound to envelopes and found predominantly in thylakoid membranes. The binding of HSP 22 was stable in the presence of high salt concentrations. Solubilization of thylakoid membranes with Triton X-100 and phase partitioning with Triton X-114 indicate an intrinsic localization of HSP 22 or, alternatively, a non-covalent association with integral membrane protein(s). After fractionation into grana and stroma lamellae, HSP 22 was found mostly in the grana-membrane subfraction.
叶绿体核编码22 kDa热休克蛋白（HSP 22）的前体已从热激处理的植物转运至分离的完整叶绿体中。对成熟蛋白在叶绿体膜中的定位进行了研究。我们发现，豌豆中经过加工的HSP 22不与包膜结合，主要存在于类囊体膜中。在高盐浓度存在的情况下，HSP 22的结合是稳定的。用Triton X - 100溶解类囊体膜并通过Triton X - 114进行相分配，表明HSP 22是内在定位，或者是与整合膜蛋白存在非共价结合。在分离为基粒和基质类囊体后发现，HSP 22主要存在于基粒膜亚组分中。
