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Sub‐cellular location of FtsH proteases in the cyanobacterium S ynechocystis sp. PCC 6803 suggests localised PSII repair zones in the thylakoid membranes

In cyanobacteria and chloroplasts, exposure to HL damages the photosynthetic apparatus, especially the D1 subunit of Photosystem II. To avoid chronic photoinhibition, a PSII repair cycle operates to replace damaged PSII subunits with newly synthesised versions. To determine the sub‐cellular location...

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Autores principales: Sacharz, Joanna, Bryan, Samantha J., Yu, Jianfeng, Burroughs, Nigel J., Spence, Edward M., Nixon, Peter J., Mullineaux, Conrad W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4949578/
https://www.ncbi.nlm.nih.gov/pubmed/25601560
http://dx.doi.org/10.1111/mmi.12940
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author Sacharz, Joanna
Bryan, Samantha J.
Yu, Jianfeng
Burroughs, Nigel J.
Spence, Edward M.
Nixon, Peter J.
Mullineaux, Conrad W.
author_facet Sacharz, Joanna
Bryan, Samantha J.
Yu, Jianfeng
Burroughs, Nigel J.
Spence, Edward M.
Nixon, Peter J.
Mullineaux, Conrad W.
author_sort Sacharz, Joanna
collection PubMed
description In cyanobacteria and chloroplasts, exposure to HL damages the photosynthetic apparatus, especially the D1 subunit of Photosystem II. To avoid chronic photoinhibition, a PSII repair cycle operates to replace damaged PSII subunits with newly synthesised versions. To determine the sub‐cellular location of this process, we examined the localisation of FtsH metalloproteases, some of which are directly involved in degrading damaged D1. We generated transformants of the cyanobacterium S ynechocystis sp. PCC6803 expressing GFP‐tagged versions of its four FtsH proteases. The ftsH2–gfp strain was functional for PSII repair under our conditions. Confocal microscopy shows that FtsH1 is mainly in the cytoplasmic membrane, while the remaining FtsH proteins are in patches either in the thylakoid or at the interface between the thylakoid and cytoplasmic membranes. HL exposure which increases the activity of the Photosystem II repair cycle led to no detectable changes in FtsH distribution, with the FtsH2 protease involved in D1 degradation retaining its patchy distribution in the thylakoid membrane. We discuss the possibility that the FtsH2–GFP patches represent Photosystem II ‘repair zones’ within the thylakoid membranes, and the possible advantages of such functionally specialised membrane zones. Anti‐GFP affinity pull‐downs provide the first indication of the composition of the putative repair zones.
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spelling pubmed-49495782016-07-28 Sub‐cellular location of FtsH proteases in the cyanobacterium S ynechocystis sp. PCC 6803 suggests localised PSII repair zones in the thylakoid membranes Sacharz, Joanna Bryan, Samantha J. Yu, Jianfeng Burroughs, Nigel J. Spence, Edward M. Nixon, Peter J. Mullineaux, Conrad W. Mol Microbiol Research Articles In cyanobacteria and chloroplasts, exposure to HL damages the photosynthetic apparatus, especially the D1 subunit of Photosystem II. To avoid chronic photoinhibition, a PSII repair cycle operates to replace damaged PSII subunits with newly synthesised versions. To determine the sub‐cellular location of this process, we examined the localisation of FtsH metalloproteases, some of which are directly involved in degrading damaged D1. We generated transformants of the cyanobacterium S ynechocystis sp. PCC6803 expressing GFP‐tagged versions of its four FtsH proteases. The ftsH2–gfp strain was functional for PSII repair under our conditions. Confocal microscopy shows that FtsH1 is mainly in the cytoplasmic membrane, while the remaining FtsH proteins are in patches either in the thylakoid or at the interface between the thylakoid and cytoplasmic membranes. HL exposure which increases the activity of the Photosystem II repair cycle led to no detectable changes in FtsH distribution, with the FtsH2 protease involved in D1 degradation retaining its patchy distribution in the thylakoid membrane. We discuss the possibility that the FtsH2–GFP patches represent Photosystem II ‘repair zones’ within the thylakoid membranes, and the possible advantages of such functionally specialised membrane zones. Anti‐GFP affinity pull‐downs provide the first indication of the composition of the putative repair zones. John Wiley and Sons Inc. 2015-02-11 2015-05 /pmc/articles/PMC4949578/ /pubmed/25601560 http://dx.doi.org/10.1111/mmi.12940 Text en © 2015 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Sacharz, Joanna
Bryan, Samantha J.
Yu, Jianfeng
Burroughs, Nigel J.
Spence, Edward M.
Nixon, Peter J.
Mullineaux, Conrad W.
Sub‐cellular location of FtsH proteases in the cyanobacterium S ynechocystis sp. PCC 6803 suggests localised PSII repair zones in the thylakoid membranes
title Sub‐cellular location of FtsH proteases in the cyanobacterium S ynechocystis sp. PCC 6803 suggests localised PSII repair zones in the thylakoid membranes
title_full Sub‐cellular location of FtsH proteases in the cyanobacterium S ynechocystis sp. PCC 6803 suggests localised PSII repair zones in the thylakoid membranes
title_fullStr Sub‐cellular location of FtsH proteases in the cyanobacterium S ynechocystis sp. PCC 6803 suggests localised PSII repair zones in the thylakoid membranes
title_full_unstemmed Sub‐cellular location of FtsH proteases in the cyanobacterium S ynechocystis sp. PCC 6803 suggests localised PSII repair zones in the thylakoid membranes
title_short Sub‐cellular location of FtsH proteases in the cyanobacterium S ynechocystis sp. PCC 6803 suggests localised PSII repair zones in the thylakoid membranes
title_sort sub‐cellular location of ftsh proteases in the cyanobacterium s ynechocystis sp. pcc 6803 suggests localised psii repair zones in the thylakoid membranes
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4949578/
https://www.ncbi.nlm.nih.gov/pubmed/25601560
http://dx.doi.org/10.1111/mmi.12940
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