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Single particle analysis of thylakoid proteins from Thermosynechococcus elongatus and Synechocystis 6803: Localization of the CupA subunit of NDH‐1
Author(s) -
Folea I. Mihaela,
Zhang Pengpeng,
Nowaczyk Marc M.,
Ogawa Teruo,
Aro Eva-Mari,
Boekema Egbert J.
Publication year - 2008
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.2007.12.012
Subject(s) - thylakoid , synechocystis , protein subunit , cyanobacteria , membrane , photosynthesis , biophysics , chloroplast , single particle analysis , electron microscope , chemistry , particle (ecology) , biochemistry , mutant , crystallography , biology , physics , bacteria , gene , ecology , organic chemistry , optics , genetics , aerosol
The larger protein complexes of the cyanobacterial photosynthetic membrane of Thermosynechoccus elongatus and Synechocystis 6803 were studied by single particle electron microscopy after detergent solubilization, without any purification steps. Besides the “standard” L‐shaped NDH‐1L complex, related to complex I, large numbers of a U‐shaped NDH‐1MS complex were found in both cyanobacteria. In membranes from Synechocystis Δ cupA and Δ cupA/cupB mutants the U‐shaped complexes were absent, indicating that CupA is responsible for the U‐shape by binding at the tip of the membrane‐bound arm of NDH‐1MS. Comparison of membranes grown under air levels of CO 2 or 3% CO 2 indicates that the number of NDH‐1MS particles is 30‐fold higher under low‐CO 2 .