Ultrastructural stability under high temperature or intensive light stress conferred by a small heat shock protein in cyanobacteria
Ultrastructural stability under high temperature or intensive light stress conferred by a small heat shock protein in cyanobacteria
复制标题
DOI：
10.1016/j.febslet.2004.12.095
复制
发表时间：
2005-02
期刊：
影响因子：
3.5
通讯作者：
K. Nitta;N. Suzuki;Daisuke Honma;Y. Kaneko;Hitoshi Nakamoto
中科院分区：
文献类型：
--
作者：
K. Nitta;N. Suzuki;Daisuke Honma;Y. Kaneko;Hitoshi Nakamoto
通过对组成表达HspA的蓝藻聚球菌菌株ECT16-1与对照菌株ECT的比较，研究了应激条件下小热休克蛋白HspA的作用和亚细胞定位。在高温或强光胁迫下，ECT细胞的超微结构出现了严重的损伤，包括细胞质聚集和类囊体膜紊乱，但在ECT16-1细胞中，这些超微结构变化不太明显。免疫细胞化学研究表明，热应激过程中，ECT16-1细胞中HspA的主要定位从类囊体区转移到细胞质区，然后再回到类囊体区。HspA的表达稳定了类核的形态。讨论了这些结果，特别是关于HspA与类囊体膜结合的独特性质。
The role and sub-cellular localization of the small heat shock protein HspA under stress conditions was investigated comparing the cyanobacterium Synechococcus strain ECT16-1, which constitutively expresses HspA, with the reference strain ECT. The ultrastructure of ECT cells under elevated temperature or intensive light stress exhibited severe damage including aggregation of cytosol and disordered thylakoid membranes, but in ECT16-1 cells these ultrastructural changes were much less conspicuous. Immunocytochemical studies showed that the main localization of HspA in the ECT16-1 cells shifted from the thylakoid area to the cytoplasm, then back to thylakoid area during the heat stress. Expression of HspA stabilized the morphology of nucleoids. The results are discussed, in particular with respect to the unique property of HspA to associate with thylakoid membranes.