The evolutionarily conserved protein PHOTOSYNTHESIS AFFECTED MUTANT71 is required for efficient manganese uptake at the thylakoid membrane in Arabidopsis

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

The evolutionarily conserved protein PHOTOSYNTHESIS AFFECTED MUTANT71 is required for efficient manganese uptake at the thylakoid membrane in Arabidopsis. / Schneider, Anja; Steinberger, Iris; Herdean, Andrei; Gandini, Chiara; Eisenhut, Marion; Kurz, Samantha; Morper, Anna; Hoecker, Natalie; Rühle, Thilo; Labs, Mathias; Flügge, Ulf Ingo; Geimer, Stefan; Schmidt, Sidsel Birkelund; Husted, Søren; Weber, Andreas P M; Spetea, Cornelia; Leister, Dario Michael.

In: Plant Cell, Vol. 28, No. 4, 2016, p. 892-910.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Schneider, A, Steinberger, I, Herdean, A, Gandini, C, Eisenhut, M, Kurz, S, Morper, A, Hoecker, N, Rühle, T, Labs, M, Flügge, UI, Geimer, S, Schmidt, SB, Husted, S, Weber, APM, Spetea, C & Leister, DM 2016, 'The evolutionarily conserved protein PHOTOSYNTHESIS AFFECTED MUTANT71 is required for efficient manganese uptake at the thylakoid membrane in Arabidopsis', Plant Cell, vol. 28, no. 4, pp. 892-910. https://doi.org/10.1105/tpc.15.00812

APA

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, S. B., Husted, S., Weber, A. P. M., Spetea, C., & Leister, D. M. (2016). The evolutionarily conserved protein PHOTOSYNTHESIS AFFECTED MUTANT71 is required for efficient manganese uptake at the thylakoid membrane in Arabidopsis. Plant Cell, 28(4), 892-910. https://doi.org/10.1105/tpc.15.00812

Vancouver

Schneider A, Steinberger I, Herdean A, Gandini C, Eisenhut M, Kurz S et al. The evolutionarily conserved protein PHOTOSYNTHESIS AFFECTED MUTANT71 is required for efficient manganese uptake at the thylakoid membrane in Arabidopsis. Plant Cell. 2016;28(4):892-910. https://doi.org/10.1105/tpc.15.00812

Author

Schneider, Anja ; Steinberger, Iris ; Herdean, Andrei ; Gandini, Chiara ; Eisenhut, Marion ; Kurz, Samantha ; Morper, Anna ; Hoecker, Natalie ; Rühle, Thilo ; Labs, Mathias ; Flügge, Ulf Ingo ; Geimer, Stefan ; Schmidt, Sidsel Birkelund ; Husted, Søren ; Weber, Andreas P M ; Spetea, Cornelia ; Leister, Dario Michael. / The evolutionarily conserved protein PHOTOSYNTHESIS AFFECTED MUTANT71 is required for efficient manganese uptake at the thylakoid membrane in Arabidopsis. In: Plant Cell. 2016 ; Vol. 28, No. 4. pp. 892-910.

Bibtex

@article{3d39634333f24fbf8d993a9f25c4c201,
title = "The evolutionarily conserved protein PHOTOSYNTHESIS AFFECTED MUTANT71 is required for efficient manganese uptake at the thylakoid membrane in Arabidopsis",
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 Mn2+ and Ca2+ 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, Mn2+ and Ca2+ ions were differently sequestered in pam71, with Ca2+ enriched in pam71 thylakoids relative to the wild type. The changes in Ca2+ 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 Mn2+, but not Ca2+. Furthermore, PAM71 suppressed the Mn2+-sensitive phenotype of the yeast mutant Δpmr1. Therefore, PAM71 presumably functions in Mn2+ uptake into thylakoids to ensure optimal PSII performance.",
author = "Anja Schneider and Iris Steinberger and Andrei Herdean and Chiara Gandini and Marion Eisenhut and Samantha Kurz and Anna Morper and Natalie Hoecker and Thilo R{\"u}hle and Mathias Labs and Fl{\"u}gge, {Ulf Ingo} and Stefan Geimer and Schmidt, {Sidsel Birkelund} and S{\o}ren Husted and Weber, {Andreas P M} and Cornelia Spetea and Leister, {Dario Michael}",
year = "2016",
doi = "10.1105/tpc.15.00812",
language = "English",
volume = "28",
pages = "892--910",
journal = "The Plant Cell",
issn = "1040-4651",
publisher = "American Society of Plant Biologists",
number = "4",

}

RIS

TY - JOUR

T1 - The evolutionarily conserved protein PHOTOSYNTHESIS AFFECTED MUTANT71 is required for efficient manganese uptake at the thylakoid membrane in Arabidopsis

AU - Schneider, Anja

AU - Steinberger, Iris

AU - Herdean, Andrei

AU - Gandini, Chiara

AU - Eisenhut, Marion

AU - Kurz, Samantha

AU - Morper, Anna

AU - Hoecker, Natalie

AU - Rühle, Thilo

AU - Labs, Mathias

AU - Flügge, Ulf Ingo

AU - Geimer, Stefan

AU - Schmidt, Sidsel Birkelund

AU - Husted, Søren

AU - Weber, Andreas P M

AU - Spetea, Cornelia

AU - Leister, Dario Michael

PY - 2016

Y1 - 2016

N2 - 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 Mn2+ and Ca2+ 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, Mn2+ and Ca2+ ions were differently sequestered in pam71, with Ca2+ enriched in pam71 thylakoids relative to the wild type. The changes in Ca2+ 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 Mn2+, but not Ca2+. Furthermore, PAM71 suppressed the Mn2+-sensitive phenotype of the yeast mutant Δpmr1. Therefore, PAM71 presumably functions in Mn2+ uptake into thylakoids to ensure optimal PSII performance.

AB - 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 Mn2+ and Ca2+ 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, Mn2+ and Ca2+ ions were differently sequestered in pam71, with Ca2+ enriched in pam71 thylakoids relative to the wild type. The changes in Ca2+ 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 Mn2+, but not Ca2+. Furthermore, PAM71 suppressed the Mn2+-sensitive phenotype of the yeast mutant Δpmr1. Therefore, PAM71 presumably functions in Mn2+ uptake into thylakoids to ensure optimal PSII performance.

U2 - 10.1105/tpc.15.00812

DO - 10.1105/tpc.15.00812

M3 - Journal article

C2 - 27020959

AN - SCOPUS:84966601425

VL - 28

SP - 892

EP - 910

JO - The Plant Cell

JF - The Plant Cell

SN - 1040-4651

IS - 4

ER -

ID: 164213217