Chloroplast Acetyltransferase NSI Is Required for State Transitions in Arabidopsis thaliana

被引:66
作者
Koskela, Minna M. [1 ]
Bruenje, Annika [2 ]
Ivanauskaite, Aiste [1 ]
Grabsztunowicz, Magda [1 ]
Lassowskat, Ines [2 ,3 ]
Neumann, Ulla [4 ]
Dinh, Trinh V. [5 ,7 ]
Sindlinger, Julia [6 ]
Schwarzer, Dirk [6 ]
Wirtz, Markus [5 ]
Tyystjaervi, Esa [1 ]
Finkemeier, Iris [2 ,3 ]
Mulo, Paula [1 ]
机构
[1] Univ Turku, Dept Biochem Mol Plant Biol, FIN-20520 Turku, Finland
[2] Univ Munster, Inst Plant Biol & Biotechnol, Plant Physiol, D-48149 Munster, Germany
[3] Max Planck Inst Plant Breeding Res, Plant Prote, D-50829 Cologne, Germany
[4] Max Planck Inst Plant Breeding Res, Cent Microscopy, D-50829 Cologne, Germany
[5] Heidelberg Univ, Ctr Organismal Studies, Dept Plant Mol Biol, D-69120 Heidelberg, Germany
[6] Univ Tubingen, Interfac Inst Biochem, D-72076 Tubingen, Germany
[7] Ind Univ Ho Chi Minh City, Inst Biotechnol & Food Technol, Ho Chi Minh City, Vietnam
基金
芬兰科学院;
关键词
HARVESTING COMPLEX-II; PHOTOSYSTEM-I; THYLAKOID MEMBRANE; LIGHT ACCLIMATION; CHLOROPHYLL-A; PSBP PROTEIN; CHLAMYDOMONAS-REINHARDTII; EXTINCTION COEFFICIENTS; COMPUTATIONAL PLATFORM; N-ACETYLTRANSFERASE;
D O I
10.1105/tpc.18.00155
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The amount of light energy received by the photosynthetic reaction centers photosystem II (PSII) and photosystem I (PSI) is balanced through state transitions. Reversible phosphorylation of a light-harvesting antenna trimer (L-LHCII) orchestrates the association between L-LHCII and the photosystems, thus adjusting the amount of excitation energy received by the reaction centers. In this study, we identified the enzyme NUCLEAR SHUTTLE INTERACTING (NSI; AT1G32070) as an active lysine acetyltransferase in the chloroplasts of Arabidopsis thaliana. Intriguingly, nsi knockout mutant plants were defective in state transitions, even though they had a similar LHCII phosphorylation pattern as the wild type. Accordingly, nsi plants were not able to accumulate the PSI-LHCII state transition complex, even though the LHCII docking site of PSI and the overall amounts of photosynthetic protein complexes remained unchanged. Instead, the nsi mutants showed a decreased Lys acetylation status of specific photosynthetic proteins including PSI, PSII, and LHCII subunits. Our work demonstrates that the chloroplast acetyltransferase NSI is needed for the dynamic reorganization of thylakoid protein complexes during photosynthetic state transitions.
引用
收藏
页码:1695 / 1709
页数:15
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