The role of Slr0151, a tetratricopeptide repeat protein from Synechocystis sp. PCC 6803, during Photosystem II assembly and repair
The assembly and repair of photosystem II (PSII) is facilitated by a variety of assembly factors. Among those, the tetratricopeptide repeat (TPR) protein Slr0151 from Synechocystis sp. PCC 6803 (hereafter Synechocystis) has previously been assigned a repair function under high light conditions (Yang...
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doaj-0a48a08a57044006801a0da4b3182ba92020-11-24T23:26:31ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2016-05-01710.3389/fpls.2016.00605192037The role of Slr0151, a tetratricopeptide repeat protein from Synechocystis sp. PCC 6803, during Photosystem II assembly and repairAnna eRast0Birgit eRengstl1Steffen eHeinz2Andreas eKlingl3Jörg eNickelsen4Ludwig-Maximillians-Universität MünchenLudwig-Maximillians-Universität MünchenLudwig-Maximillians-Universität MünchenLudwig-Maximilians-Universität MünchenLudwig-Maximillians-Universität MünchenThe assembly and repair of photosystem II (PSII) is facilitated by a variety of assembly factors. Among those, the tetratricopeptide repeat (TPR) protein Slr0151 from Synechocystis sp. PCC 6803 (hereafter Synechocystis) has previously been assigned a repair function under high light conditions (Yang et al., 2014, J. Integr. Plant Biol. 56, 1136-50). Here, we show that inactivation of Slr0151 affects thylakoid membrane ultrastructure even under normal light conditions. Moreover, the level and localization of Slr0151 are affected in a variety of PSII-related mutants. In particular, the data suggest a close functional relationship between Slr0151 and Sll0933, which interacts with Ycf48 during PSII assembly and is homologous to PAM68 in Arabidopsis thaliana. Immunofluorescence analysis revealed a punctate distribution of Slr0151 within several different membrane types in Synechocystis cells.http://journal.frontiersin.org/Journal/10.3389/fpls.2016.00605/fullSynechocystisphotosystem IIthylakoid membranebiogenesis centerTPR protein |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Anna eRast Birgit eRengstl Steffen eHeinz Andreas eKlingl Jörg eNickelsen |
spellingShingle |
Anna eRast Birgit eRengstl Steffen eHeinz Andreas eKlingl Jörg eNickelsen The role of Slr0151, a tetratricopeptide repeat protein from Synechocystis sp. PCC 6803, during Photosystem II assembly and repair Frontiers in Plant Science Synechocystis photosystem II thylakoid membrane biogenesis center TPR protein |
author_facet |
Anna eRast Birgit eRengstl Steffen eHeinz Andreas eKlingl Jörg eNickelsen |
author_sort |
Anna eRast |
title |
The role of Slr0151, a tetratricopeptide repeat protein from Synechocystis sp. PCC 6803, during Photosystem II assembly and repair |
title_short |
The role of Slr0151, a tetratricopeptide repeat protein from Synechocystis sp. PCC 6803, during Photosystem II assembly and repair |
title_full |
The role of Slr0151, a tetratricopeptide repeat protein from Synechocystis sp. PCC 6803, during Photosystem II assembly and repair |
title_fullStr |
The role of Slr0151, a tetratricopeptide repeat protein from Synechocystis sp. PCC 6803, during Photosystem II assembly and repair |
title_full_unstemmed |
The role of Slr0151, a tetratricopeptide repeat protein from Synechocystis sp. PCC 6803, during Photosystem II assembly and repair |
title_sort |
role of slr0151, a tetratricopeptide repeat protein from synechocystis sp. pcc 6803, during photosystem ii assembly and repair |
publisher |
Frontiers Media S.A. |
series |
Frontiers in Plant Science |
issn |
1664-462X |
publishDate |
2016-05-01 |
description |
The assembly and repair of photosystem II (PSII) is facilitated by a variety of assembly factors. Among those, the tetratricopeptide repeat (TPR) protein Slr0151 from Synechocystis sp. PCC 6803 (hereafter Synechocystis) has previously been assigned a repair function under high light conditions (Yang et al., 2014, J. Integr. Plant Biol. 56, 1136-50). Here, we show that inactivation of Slr0151 affects thylakoid membrane ultrastructure even under normal light conditions. Moreover, the level and localization of Slr0151 are affected in a variety of PSII-related mutants. In particular, the data suggest a close functional relationship between Slr0151 and Sll0933, which interacts with Ycf48 during PSII assembly and is homologous to PAM68 in Arabidopsis thaliana. Immunofluorescence analysis revealed a punctate distribution of Slr0151 within several different membrane types in Synechocystis cells. |
topic |
Synechocystis photosystem II thylakoid membrane biogenesis center TPR protein |
url |
http://journal.frontiersin.org/Journal/10.3389/fpls.2016.00605/full |
work_keys_str_mv |
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