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The exposed N-terminal tail of the D1 subunit is required for rapid D1 degradation during photosystem II repair in Synechocystis sp PCC 6803
J Komenda, M Tichy, O Prasil, J Knoppova, S Kuvikova, Vries R de, PJ Nixon
Language English Country United States
NLK
Free Medical Journals
from 1989 to 1 year ago
Freely Accessible Science Journals
from 1989 to 12 months ago
ProQuest Central
from 1998-12-01 to 2012-08-31
Open Access Digital Library
from 1989-01-01
Health & Medicine (ProQuest)
from 1998-12-01 to 2012-08-31
- MeSH
- Autotrophic Processes drug effects radiation effects MeSH
- Models, Biological MeSH
- Dimerization MeSH
- Financing, Organized MeSH
- Spectrometry, Fluorescence MeSH
- Photosystem II Protein Complex genetics chemistry MeSH
- Lincomycin pharmacology MeSH
- Molecular Sequence Data MeSH
- Mutation genetics MeSH
- Mutant Proteins metabolism MeSH
- Protein Subunits chemistry metabolism MeSH
- Protein Processing, Post-Translational drug effects radiation effects MeSH
- Protein Structure, Secondary MeSH
- Amino Acid Sequence MeSH
- Light MeSH
- Synechocystis MeSH
- Thylakoids metabolism drug effects radiation effects MeSH
- Structure-Activity Relationship MeSH
The selective replacement of photodamaged D1 protein within the multisubunit photosystem II (PSII) complex is an important photoprotective mechanism in chloroplasts and cyanobacteria. FtsH proteases are involved at an early stage of D1 degradation, but it remains unclear how the damaged D1 subunit is recognized, degraded, and replaced. To test the role of the N-terminal region of D1 in PSII biogenesis and repair, we have constructed mutants of the cyanobacterium Synechocystis sp PCC 6803 that are truncated at the exposed N terminus. Removal of 5 or 10 residues blocked D1 synthesis, as assessed in radiolabeling experiments, whereas removal of 20 residues restored the ability to assemble oxygen-evolving dimeric PSII complexes but inhibited PSII repair at the level of D1 degradation. Overall, our results identify an important physiological role for the exposed N-terminal tail of D1 at an early step in selective D1 degradation. This finding has important implications for the recognition of damaged D1 and its synchronized replacement by a newly synthesized subunit.
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- $a Institute of Microbiology, Academy of Sciences, Opatovicky mlyn, 37981, Trebon, Czech Republic. komenda@alga.cz
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- $a The selective replacement of photodamaged D1 protein within the multisubunit photosystem II (PSII) complex is an important photoprotective mechanism in chloroplasts and cyanobacteria. FtsH proteases are involved at an early stage of D1 degradation, but it remains unclear how the damaged D1 subunit is recognized, degraded, and replaced. To test the role of the N-terminal region of D1 in PSII biogenesis and repair, we have constructed mutants of the cyanobacterium Synechocystis sp PCC 6803 that are truncated at the exposed N terminus. Removal of 5 or 10 residues blocked D1 synthesis, as assessed in radiolabeling experiments, whereas removal of 20 residues restored the ability to assemble oxygen-evolving dimeric PSII complexes but inhibited PSII repair at the level of D1 degradation. Overall, our results identify an important physiological role for the exposed N-terminal tail of D1 at an early step in selective D1 degradation. This finding has important implications for the recognition of damaged D1 and its synchronized replacement by a newly synthesized subunit.
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