Removal of both Ycf48 and Psb27 in Synechocystis sp. PCC 6803 disrupts Photosystem II assembly and alters QA− oxidation in the mature complex. Issue 20 (27th August 2014)
- Record Type:
- Journal Article
- Title:
- Removal of both Ycf48 and Psb27 in Synechocystis sp. PCC 6803 disrupts Photosystem II assembly and alters QA− oxidation in the mature complex. Issue 20 (27th August 2014)
- Main Title:
- Removal of both Ycf48 and Psb27 in Synechocystis sp. PCC 6803 disrupts Photosystem II assembly and alters QA− oxidation in the mature complex
- Authors:
- Jackson, Simon A.
Hervey, John R.D.
Dale, Asher J.
Eaton-Rye, Julian J. - Abstract:
- Abstract : The Photosystem II (PS II) assembly factors Psb27 and Ycf48 are transiently associated with PS II during its biogenesis and repair pathways. We investigated the function of these proteins by constructing knockout mutants in Synechocystis sp. PCC 6803. In ΔYcf48 cells, PS II electron transfer and stable oxygen evolution were perturbed. Additionally, Psb27 was required for photoautotrophic growth of cells lacking Ycf48 and assembly beyond the RC47 assembly complex in ΔYcf48:ΔPsb27 cells was impeded. Our results suggest the RC47 complex formed in ΔYcf48 cells is defective and that this deficiency is exacerbated if CP43 binds in the absence of Psb27. Abstract : Photosystem II assembly has been studied in a ΔYcf48:ΔPsb27 double deletion mutant. Photoautotrophic growth and oxygen evolution were impaired in ΔYcf48:ΔPsb27 cells. Electron transfer in the presence and absence of DCMU was modified in the single and double mutants. Photosystem II sub‐complexes accumulated in the ΔYcf48:ΔPsb27 strain. An assembly "bottleneck" at the level of the RC47 sub‐complex was observed.
- Is Part Of:
- FEBS letters. Volume 588:Issue 20(2014)
- Journal:
- FEBS letters
- Issue:
- Volume 588:Issue 20(2014)
- Issue Display:
- Volume 588, Issue 20 (2014)
- Year:
- 2014
- Volume:
- 588
- Issue:
- 20
- Issue Sort Value:
- 2014-0588-0020-0000
- Page Start:
- 3751
- Page End:
- 3760
- Publication Date:
- 2014-08-27
- Subjects:
- Bis–Tris -- 2-[bis(2-hydroxyethyl)amino]-2-(hydroxymethyl)-propane-1, 3-diol -- BSA -- bovine serum albumin -- BMF -- blue measuring flashes -- BN-PAGE -- blue-native polyacrylamide gel electrophoresis -- CP43 -- 43-kDa chlorophyll a-binding protein of the core antenna -- CP47 -- 47-kDa chlorophyll a-binding protein of the core antenna -- D1 -- Photosystem II reaction center protein subunit -- D2 -- Photosystem II reaction center protein subunit -- DCBQ -- 2, 6-dichloro-1, 4-benzoquinone -- DCMU -- 3-(3, 4-dichlorophenyl)-1, 1-dimethylurea -- ECL -- enhanced chemiluminescence -- HEPES -- 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid -- iD1 -- intermediate form of the D1 protein -- OCP -- orange carotenoid protein -- OD -- optical density -- pD1 -- precursor form of the D1 protein -- PDM -- PratA-defined membrane -- PS II -- Photosystem II -- QA -- primary plastoquinone electron acceptor of PS II -- QB -- secondary plastoquinone electron acceptor of PS II -- RC -- reaction center -- RCII -- reaction center pre-complex containing D1, D2, cytochrome b559 and Ycf48 -- RC47 -- reaction center complex lacking the CP43 protein -- RMF -- red measuring flashes -- SLIC -- sequence and ligation independent cloning -- TES -- N-[tris(hydroxymethyl)methyl]-2-aminoethanesulfonic acid -- Tris -- 2-amino-2-hydroxymethyl-propane-1, 3-diol -- Assembly -- Biogenesis -- Photosystem II -- Psb27 -- Synechocystis sp. PCC 6803 -- Ycf48
Biochemistry -- Periodicals
Biophysics -- Periodicals
Molecular biology -- Periodicals
Biochimie -- Périodiques
Biochemistry
Biophysics
Molecular biology
Periodicals
572.05 - Journal URLs:
- http://www.sciencedirect.com/science/journal/00145793 ↗
http://febs.onlinelibrary.wiley.com/hub/journal/10.1002/(ISSN)1873-3468/ ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.febslet.2014.08.024 ↗
- Languages:
- English
- ISSNs:
- 0014-5793
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3901.600000
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