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Ultrastructural stability under high temperature or intensive light stress conferred by a small heat shock protein in cyanobacteria
Author(s) -
Nitta Koji,
Suzuki Nobuaki,
Honma Daisuke,
Kaneko Yasuko,
Nakamoto Hitoshi
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.12.095
Subject(s) - thylakoid , ultrastructure , nucleoid , cytoplasm , heat shock protein , microbiology and biotechnology , cytosol , chloroplast , biophysics , cyanobacteria , biology , chemistry , biochemistry , botany , gene , bacteria , genetics , escherichia coli , enzyme
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.