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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Main Authors: Anna eRast, Birgit eRengstl, Steffen eHeinz, Andreas eKlingl, Jörg eNickelsen
Format: Article
Language:English
Published: Frontiers Media S.A. 2016-05-01
Series:Frontiers in Plant Science
Subjects:
Online Access:http://journal.frontiersin.org/Journal/10.3389/fpls.2016.00605/full
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spelling 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
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