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Effect of Chlamydomonas plastid terminal oxidase 1 expressed in tobacco on photosynthetic electron transfer
Author(s) -
Feilke Kathleen,
Streb Peter,
Cornic Gabriel,
Perreau François,
Kruk Jerzy,
KriegerLiszkay Anja
Publication year - 2016
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/tpj.13101
Subject(s) - thylakoid , chlamydomonas reinhardtii , electron transport chain , photosynthesis , electron transfer , plastid , photoinhibition , chemistry , biophysics , biochemistry , biology , photochemistry , chloroplast , photosystem ii , mutant , gene
Summary The plastid terminal oxidase PTOX is a plastohydroquinone:oxygen oxidoreductase that is important for carotenoid biosynthesis and plastid development. Its role in photosynthesis is controversially discussed. Under a number of abiotic stress conditions, the protein level of PTOX increases. PTOX is thought to act as a safety valve under high light protecting the photosynthetic apparatus against photodamage. However, transformants with high PTOX level were reported to suffer from photoinhibition. To analyze the effect of PTOX on the photosynthetic electron transport, tobacco expressing PTOX ‐1 from Chlamydomonas reinhardtii (Cr‐ PTOX 1) was studied by chlorophyll fluorescence, thermoluminescence, P700 absorption kinetics and CO 2 assimilation. Cr‐ PTOX 1 was shown to compete very efficiently with the photosynthetic electron transport for PQH 2 . High pressure liquid chromatography ( HPLC ) analysis confirmed that the PQ pool was highly oxidized in the transformant. Immunoblots showed that, in the wild‐type, PTOX was associated with the thylakoid membrane only at a relatively alkaline pH value while it was detached from the membrane at neutral pH . We present a model proposing that PTOX associates with the membrane and oxidizes PQH 2 only when the oxidation of PQH 2 by the cytochrome b 6 f complex is limiting forward electron transport due to a high proton gradient across the thylakoid membrane.