Light acclimation involves dynamic re‐organization of the pigment–protein megacomplexes in non‐appressed thylakoid domains

Marjaana Suorsa; Marjaana Rantala; Fikret Mamedov; Maija Lespinasse; Andrea Trotta; Michele Grieco; Eerika Vuorio; Mikko Tikkanen; Sari Järvi; Eva‐Mari Aro

doi:10.1111/tpj.13004

journal article Open Access Oct 01, 2015

Light acclimation involves dynamic re‐organization of the pigment–protein megacomplexes in non‐appressed thylakoid domains

Marjaana Suorsa Marjaana Rantala Fikret Mamedov Maija Lespinasse Andrea Trotta

Michele Grieco Eerika Vuorio Mikko Tikkanen Sari Järvi Eva‐Mari Aro

The Plant Journal Vol. 84 No. 2 pp. 360-373 · Wiley

View at Publisher Save 10.1111/tpj.13004

Abstract

SummaryThylakoid energy metabolism is crucial for plant growth, development and acclimation. Non‐appressed thylakoids harbor several high molecular mass pigment–protein megacomplexes that have flexible compositions depending upon the environmental cues. This composition is important for dynamic energy balancing in photosystems (PS) I and II. We analysed the megacomplexes of Arabidopsis wild type (WT) plants and of several thylakoid regulatory mutants. The stn7 mutant, which is defective in phosphorylation of the light‐harvesting complex (LHC) II, possessed a megacomplex composition that was strikingly different from that of the WT. Of the nine megacomplexes in total for the non‐appressed thylakoids, the largest megacomplex in particular was less abundant in the stn7 mutant under standard growth conditions. This megacomplex contains both PSI and PSII and was recently shown to allow energy spillover between PSII and PSI (Nat. Commun., 6, 2015, 6675). The dynamics of the megacomplex composition was addressed by exposing plants to different light conditions prior to thylakoid isolation. The megacomplex pattern in the WT was highly dynamic. Under darkness or far red light it showed low levels of LHCII phosphorylation and resembled the stn7 pattern; under low light, which triggers LHCII phosphorylation, it resembled that of the tap38/pph1 phosphatase mutant. In contrast, solubilization of the entire thylakoid network with dodecyl maltoside, which efficiently solubilizes pigment–protein complexes from all thylakoid compartments, revealed that the pigment–protein composition remained stable despite the changing light conditions or mutations that affected LHCII (de)phosphorylation. We conclude that the composition of pigment–protein megacomplexes specifically in non‐appressed thylakoids undergoes redox‐dependent changes, thus facilitating maintenance of the excitation balance between the two photosystems upon changes in light conditions.

Topics

No keywords indexed for this article. Browse by subject →

References

78

[1]

10.1016/s1360-1385(01)02021-0

[2]

10.1098/rstb.2012.0373

[3]

10.1105/tpc.113.113118

[4]

10.1038/nature03286

[5]

10.1105/tpc.109.069815

[6]

10.1038/nature04016

[7]

10.1105/tpc.108.062018

[8]

10.1038/emboj.2009.232

[9]

10.1016/j.bbabio.2008.10.002

[10]

10.1016/j.bbabio.2003.10.005

[11]

10.1016/j.bbabio.2004.09.009

[12]

10.1105/tpc.111.087049

[13]

10.1111/j.1399-3054.2006.00831.x

[14]

10.1105/tpc.112.100339

[15]

10.1073/pnas.0507287103

[16]

10.1016/j.jplph.2014.03.004

[17]

10.1104/pp.112.206466

[18]

10.1016/j.bbabio.2015.03.004

[19]

10.1007/bf00019047

[20]

10.1093/nar/gkl863

[21]

Proteomic approach to characterize the supramolecular organization of photosystems in higher plants

Jesco Heinemeyer, Holger Eubel, Dirk Wehmhöner et al.

Phytochemistry 10.1016/j.phytochem.2004.04.022

[22]

10.1073/pnas.1214265109

[23]

10.1038/srep03768

[24]

10.1042/bj20102155

[25]

10.1016/j.bbabio.2015.01.006

[26]

Kettunen R. (1995)

[27]

10.1007/s11120-013-9843-0

[28]

10.1021/bi011650y

[29]

10.1021/bi0494626

[30]

The Arabidopsis thaliana Chloroplast Proteome Reveals Pathway Abundance and Novel Protein Functions

Torsten Kleffmann, Doris Russenberger, Anne von Zychlinski et al.

Current Biology 10.1016/j.cub.2004.02.039

[31]

10.1093/pcp/pcu033

[32]

10.1016/j.bbabio.2012.12.003

[33]

10.1007/s004250050583

[34]

10.1007/s00425-002-0790-9

[35]

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

U. K. LAEMMLI

Nature 10.1038/227680a0

[36]

10.1007/bf00021793

[37]

10.3389/fpls.2013.00161

[38]

10.1111/tpj.12297

[39]

10.1038/35000131

[40]

10.1073/pnas.232447699

[41]

10.1111/nph.12622

[42]

10.1093/mp/sst129

[43]

10.1105/tpc.111.085456

[44]

10.1038/35046121

[45]

10.1016/s0092-8674(02)00867-x

[46]

10.1146/annurev-arplant-050312-120124

[47]

10.1016/s0168-9452(00)00337-x

[48]

10.1016/j.bbabio.2013.11.004

[49]

Central Functions of the Lumenal and Peripheral Thylakoid Proteome of Arabidopsis Determined by Experimentation and Genome-Wide Prediction

Jean-Benoît Peltier, Olof Emanuelsson, Dário E. Kalume et al.

The Plant Cell 10.1105/tpc.010304

[50]

10.1074/jbc.m803207200

Showing 50 of 78 references

Metrics

75

Citations

78

References

Details

Published: Oct 01, 2015
Vol/Issue: 84(2)
Pages: 360-373
License: View

Authors

M

Marjaana Suorsa