Accumulation of water oxidation polypeptides in PSII mutants
Conference
·
· Plant Physiol., Suppl.; (United States)
OSTI ID:5095952
Cytoplasmically synthesized extrinsic thylakoid proteins of 29, 20, and 16 kD in Chlamydomonas are homologous to the 33, 24, and 18 kD polypeptides of higher plant water oxidation complexes. Three photosystem II mutants of Chlamydomonas do not accumulate components of PSII reaction centers as a consequence of single nuclear (GE2.10, F34) or plastome (8-36c) lesions. Thylakoids purified from these strains also show a deficiency of the three polypeptides of the oxygen evolution complex. Whole cell extracts, on the other hand, reveal that the polypeptides accumulate to nearly wild type levels and comigrate on one and two dimensional gels with the mature forms found in wild type cells. Thus, precursors are correctly processed even in the absence of PSII reaction centers. Because the polypeptides are absent from purified mutant thylakoids it can be concluded that binding of the complex to thylakoids is impaired by lack of PSII reaction center polypeptides. Preliminary immunocytochemical localization indicates a similar distribution of at least one of these polypeptides in mutant and wild type chloroplasts.
- Research Organization:
- Univ. of Georgia, Athens
- OSTI ID:
- 5095952
- Conference Information:
- Journal Name: Plant Physiol., Suppl.; (United States) Journal Volume: 80:4
- Country of Publication:
- United States
- Language:
- English
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