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Salar Torabi Pavan Umate Nikolay Manavski Magdalena Pl?chinger Laura Kleinknecht Hanumakumar Bogireddi Reinhold G. Herrmann Gerhard Wanner Wolfgang P. Schr?der J?rg Meurer 《The Plant cell》2014,26(3):1183-1199
The chloroplast-encoded low molecular weight protein PsbN is annotated as a
photosystem II (PSII) subunit. To elucidate
the localization and function of PsbN, encoded on the opposite strand to the
psbB gene cluster, we raised antibodies and inserted a resistance
cassette into PsbN in both directions. Both homoplastomic tobacco
(Nicotiana tabacum) mutants ∆psbN-F and
∆psbN-R show essentially the same PSII deficiencies. The mutants are extremely light sensitive and
failed to recover from photoinhibition. Although synthesis of PSII proteins was not altered significantly, both mutants
accumulated only ∼25% of PSII proteins
compared with the wild type. Assembly of PSII
precomplexes occurred at normal rates, but heterodimeric PSII reaction centers (RCs) and higher order PSII
assemblies were not formed efficiently in the mutants. The
∆psbN-R mutant was complemented by allotopic expression of
the PsbN gene fused to the sequence of a chloroplast transit peptide
in the nuclear genome. PsbN represents a bitopic trans-membrane
peptide localized in stroma lamellae with its highly conserved C terminus exposed to
the stroma. Significant amounts of PsbN were already present in dark-grown seedling.
Our data prove that PsbN is not a constituent subunit of PSII but is required for repair from photoinhibition and
efficient assembly of the PSII
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