The Evolutionarily Conserved Protein PHOTOSYNTHESIS AFFECTED MUTANT71 Is Required for Efficient Manganese Uptake at the Thylakoid Membrane in Arabidopsis.

Schneider, A; Steinberger, I; Herdean, A; Gandini, C; Eisenhut, M; Kurz, S; Morper, A; Hoecker, N; Rühle, T; Labs, M; Flügge, U-I; Geimer, S; Schmidt, SB; Husted, S; Weber, APM; Spetea, C; Leister, D

The Evolutionarily Conserved Protein PHOTOSYNTHESIS AFFECTED MUTANT71 Is Required for Efficient Manganese Uptake at the Thylakoid Membrane in Arabidopsis.

Schneider, A Steinberger, I Herdean, A

Gandini, C Eisenhut, M Kurz, S Morper, A Hoecker, N Rühle, T Labs, M Flügge, U-I Geimer, S Schmidt, SB Husted, S Weber, APM Spetea, C Leister, D

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Publisher:: AMER SOC PLANT BIOLOGISTS
Publication Type:: Journal Article
Citation:: Plant Cell, 2016, 28, (4), pp. 892-910
Issue Date:: 2016-04

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Field	Value	Language
dc.contributor.author	Schneider, A
dc.contributor.author	Steinberger, I
dc.contributor.author	Herdean, A https://orcid.org/0000-0003-2143-0213
dc.contributor.author	Gandini, C
dc.contributor.author	Eisenhut, M
dc.contributor.author	Kurz, S
dc.contributor.author	Morper, A
dc.contributor.author	Hoecker, N
dc.contributor.author	Rühle, T
dc.contributor.author	Labs, M
dc.contributor.author	Flügge, U-I
dc.contributor.author	Geimer, S
dc.contributor.author	Schmidt, SB
dc.contributor.author	Husted, S
dc.contributor.author	Weber, APM
dc.contributor.author	Spetea, C
dc.contributor.author	Leister, D
dc.date.accessioned	2022-08-15T21:02:52Z
dc.date.available	2016-03-24
dc.date.available	2022-08-15T21:02:52Z
dc.date.issued	2016-04
dc.identifier.citation	Plant Cell, 2016, 28, (4), pp. 892-910
dc.identifier.issn	1040-4651
dc.identifier.issn	1532-298X
dc.identifier.uri	http://hdl.handle.net/10453/160247
dc.description.abstract	In plants, algae, and cyanobacteria, photosystem II (PSII) catalyzes the light-driven oxidation of water. The oxygen-evolving complex of PSII is a Mn4CaO5 cluster embedded in a well-defined protein environment in the thylakoid membrane. However, transport of manganese and calcium into the thylakoid lumen remains poorly understood. Here, we show that Arabidopsis thaliana PHOTOSYNTHESIS AFFECTED MUTANT71 (PAM71) is an integral thylakoid membrane protein involved in Mn(2+) and Ca(2+) homeostasis in chloroplasts. This protein is required for normal operation of the oxygen-evolving complex (as evidenced by oxygen evolution rates) and for manganese incorporation. Manganese binding to PSII was severely reduced in pam71 thylakoids, particularly in PSII supercomplexes. In cation partitioning assays with intact chloroplasts, Mn(2+) and Ca(2+) ions were differently sequestered in pam71, with Ca(2+) enriched in pam71 thylakoids relative to the wild type. The changes in Ca(2+) homeostasis were accompanied by an increased contribution of the transmembrane electrical potential to the proton motive force across the thylakoid membrane. PSII activity in pam71 plants and the corresponding Chlamydomonas reinhardtii mutant cgld1 was restored by supplementation with Mn(2+), but not Ca(2+) Furthermore, PAM71 suppressed the Mn(2+)-sensitive phenotype of the yeast mutant Δpmr1 Therefore, PAM71 presumably functions in Mn(2+) uptake into thylakoids to ensure optimal PSII performance.
dc.format	Print-Electronic
dc.language	eng
dc.publisher	AMER SOC PLANT BIOLOGISTS
dc.relation.ispartof	Plant Cell
dc.relation.isbasedon	10.1105/tpc.15.00812
dc.rights	info:eu-repo/semantics/closedAccess
dc.subject	0601 Biochemistry and Cell Biology, 0604 Genetics, 0607 Plant Biology
dc.subject.classification	Plant Biology & Botany
dc.subject.mesh	Arabidopsis
dc.subject.mesh	Arabidopsis Proteins
dc.subject.mesh	Calcium
dc.subject.mesh	Chlamydomonas reinhardtii
dc.subject.mesh	Chloroplasts
dc.subject.mesh	Manganese
dc.subject.mesh	Thylakoid Membrane Proteins
dc.subject.mesh	Thylakoids
dc.subject.mesh	Chloroplasts
dc.subject.mesh	Thylakoids
dc.subject.mesh	Chlamydomonas reinhardtii
dc.subject.mesh	Arabidopsis
dc.subject.mesh	Calcium
dc.subject.mesh	Manganese
dc.subject.mesh	Arabidopsis Proteins
dc.subject.mesh	Thylakoid Membrane Proteins
dc.title	The Evolutionarily Conserved Protein PHOTOSYNTHESIS AFFECTED MUTANT71 Is Required for Efficient Manganese Uptake at the Thylakoid Membrane in Arabidopsis.
dc.type	Journal Article
utslib.citation.volume	28
utslib.location.activity	England
utslib.for	0601 Biochemistry and Cell Biology
utslib.for	0604 Genetics
utslib.for	0607 Plant Biology
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - C3 - Climate Change Cluster
utslib.copyright.status	closed_access	*
dc.date.updated	2022-08-15T21:02:50Z
pubs.issue	4
pubs.publication-status	Published
pubs.volume	28
utslib.citation.issue	4

Abstract:

In plants, algae, and cyanobacteria, photosystem II (PSII) catalyzes the light-driven oxidation of water. The oxygen-evolving complex of PSII is a Mn4CaO5 cluster embedded in a well-defined protein environment in the thylakoid membrane. However, transport of manganese and calcium into the thylakoid lumen remains poorly understood. Here, we show that Arabidopsis thaliana PHOTOSYNTHESIS AFFECTED MUTANT71 (PAM71) is an integral thylakoid membrane protein involved in Mn(2+) and Ca(2+) homeostasis in chloroplasts. This protein is required for normal operation of the oxygen-evolving complex (as evidenced by oxygen evolution rates) and for manganese incorporation. Manganese binding to PSII was severely reduced in pam71 thylakoids, particularly in PSII supercomplexes. In cation partitioning assays with intact chloroplasts, Mn(2+) and Ca(2+) ions were differently sequestered in pam71, with Ca(2+) enriched in pam71 thylakoids relative to the wild type. The changes in Ca(2+) homeostasis were accompanied by an increased contribution of the transmembrane electrical potential to the proton motive force across the thylakoid membrane. PSII activity in pam71 plants and the corresponding Chlamydomonas reinhardtii mutant cgld1 was restored by supplementation with Mn(2+), but not Ca(2+) Furthermore, PAM71 suppressed the Mn(2+)-sensitive phenotype of the yeast mutant Δpmr1 Therefore, PAM71 presumably functions in Mn(2+) uptake into thylakoids to ensure optimal PSII performance.

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http://hdl.handle.net/10453/160247