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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
Jazyk angličtina Země Spojené státy americké
NLK
Free Medical Journals
od 1989 do Před 1 rokem
Freely Accessible Science Journals
od 1989 do Před 12 měsíci
ProQuest Central
od 1998-12-01 do 2012-08-31
Open Access Digital Library
od 1989-01-01
Health & Medicine (ProQuest)
od 1998-12-01 do 2012-08-31
- MeSH
- autotrofní procesy účinky léků účinky záření MeSH
- biologické modely MeSH
- dimerizace MeSH
- financování organizované MeSH
- fluorescenční spektrometrie MeSH
- fotosystém II (proteinový komplex) genetika chemie MeSH
- linkomycin farmakologie MeSH
- molekulární sekvence - údaje MeSH
- mutace genetika MeSH
- mutantní proteiny metabolismus MeSH
- podjednotky proteinů chemie metabolismus MeSH
- posttranslační úpravy proteinů účinky léků účinky záření MeSH
- sekundární struktura proteinů MeSH
- sekvence aminokyselin MeSH
- světlo MeSH
- Synechocystis MeSH
- tylakoidy metabolismus účinky léků účinky záření MeSH
- vztahy mezi strukturou a aktivitou 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 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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