G. Nagy, as revealed by noninvasive techniques in vivo, Proceedings of the National Academy of Sciences, vol.111, issue.13, pp.5042-5047, 2014.
DOI : 10.1074/jbc.M809360200
URL : https://hal.archives-ouvertes.fr/hal-00984403

C. Ünlü, B. Drop, R. Croce, and H. Van-amerongen, strongly modulate the functional size of photosystem II but not of photosystem I, Proceedings of the National Academy of Sciences, vol.111, issue.9, pp.3460-3465, 2014.
DOI : 10.1105/tpc.104.025387

W. Nawrocki, S. Santabarbara, L. Mosebach, F. Wollman, and F. Rappaport, State transitions redistribute rather than dissipate energy between the two photosystems in Chlamydomonas, Nature Plants, vol.4, issue.4, p.16031, 2016.
DOI : 10.1074/jbc.M111.331991

O. Canaani, J. Barber, and S. Malkin, Evidence that phosphorylation and dephosphorylation regulate the distribution of excitation energy between the two photosystems of photosynthesis in vivo: Photoacoustic and fluorimetric study of an intact leaf, Proceedings of the National Academy of Sciences, vol.81, issue.6, pp.1614-1618, 1984.
DOI : 10.1073/pnas.81.6.1614

O. Canaani and S. Malkin, Distribution of light excitation in an intact leaf between the two photosystems of photosynthesis. Changes in absorption cross-sections following state 1-state 2 transitions, Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol.766, issue.3, pp.513-524, 1984.
DOI : 10.1016/0005-2728(84)90109-9

M. Fleischmann, Deficient in State Transition, Journal of Biological Chemistry, vol.545, issue.43, pp.30987-30994, 1999.
DOI : 10.1083/jcb.103.1.71

H. Takahashi, S. Clowez, F. Wollman, O. Vallon, and F. Rappaport, Cyclic electron flow is redox-controlled but independent of state transition, Nature Communications, vol.23, 1954.
DOI : 10.1111/j.1365-3040.2007.01680.x

L. Dumas, M. Chazaux, G. Peltier, X. Johnson, and J. Alric, Cytochrome b 6 f function and localization, phosphorylation state of thylakoid membrane proteins and consequences on cyclic electron flow, Photosynthesis Research, vol.42, issue.42, pp.307-320, 2016.
DOI : 10.1021/bi0350957

J. Allen, J. Bennett, K. Steinback, and C. Arntzen, Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems, Nature, vol.502, issue.5810, pp.25-29, 1981.
DOI : 10.1038/291025a0

F. Wollman and C. Lemaire, Studies on kinase-controlled state transitions in Photosystem II and b6f mutants from Chlamydomonas reinhardtii which lack quinone-binding proteins, Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol.933, issue.1, pp.85-94, 1988.
DOI : 10.1016/0005-2728(88)90058-8

J. Bennett, Phosphorylation of chloroplast membrane polypeptides, Nature, vol.175, issue.5626, pp.344-346, 1977.
DOI : 10.1042/bj1300901a

P. Horton, J. Allen, M. Black, and J. Bennett, Regulation of phosphorylation of chloroplast membrane polypeptides by the redox state of plastoquinone, FEBS Letters, vol.189, issue.2, pp.193-196, 1981.
DOI : 10.1016/0005-2728(69)90168-6

B. Andersson and J. Anderson, Lateral heterogeneity in the distribution of chlorophyll-protein complexes of the thylakoid membranes of spinach chloroplasts, Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol.593, issue.2, pp.427-440, 1980.
DOI : 10.1016/0005-2728(80)90078-X

N. Depège, S. Bellafiore, and J. Rochaix, Role of Chloroplast Protein Kinase Stt7 in LHCII Phosphorylation and State Transition in Chlamydomonas, Science, vol.299, issue.5612, pp.1572-1575, 2003.
DOI : 10.1126/science.1081397

A. Shapiguzov, The PPH1 phosphatase is specifically involved in LHCII dephosphorylation and state transitions in Arabidopsis, Proceedings of the National Academy of Sciences, vol.50, issue.10, pp.4782-4787, 2010.
DOI : 10.1093/pcp/pcp122

M. Pribil, P. Pesaresi, A. Hertle, R. Barbato, and D. Leister, Role of Plastid Protein Phosphatase TAP38 in LHCII Dephosphorylation and Thylakoid Electron Flow, PLoS Biology, vol.238, issue.1, p.1000288, 2010.
DOI : 10.1371/journal.pbio.1000288.s002

A. Vener, P. Van-kan, A. Gal, B. Andersson, and I. Ohad, Activation/Deactivation Cycle of Redox-controlled Thylakoid Protein Phosphorylation, Journal of Biological Chemistry, vol.2, issue.42, pp.25225-25232, 1995.
DOI : 10.1111/j.1751-1097.1995.tb09237.x

F. Zito, The Qo site of cytochrome b6f complexes controls the activation of the LHCII kinase, The EMBO Journal, vol.18, issue.11, pp.2961-2969, 1999.
DOI : 10.1093/emboj/18.11.2961

P. Hamel, J. Olive, Y. Pierre, F. Wollman, and C. De-vitry, Complex Undergoes Reversible Phosphorylation upon State Transition, Journal of Biological Chemistry, vol.974, issue.22, pp.17072-17079, 2000.
DOI : 10.1104/pp.108.2.787
URL : http://www.jbc.org/content/275/22/17072.full.pdf

S. Lemeille, Analysis of the Chloroplast Protein Kinase Stt7 during State Transitions, PLoS Biology, vol.75, issue.3, p.45, 2009.
DOI : 10.1371/journal.pbio.1000045.sd001
URL : https://hal.archives-ouvertes.fr/hal-00412928

C. De-vitry, Y. Ouyang, G. Finazzi, F. Wollman, and T. Kallas, The Chloroplast Rieske Iron-Sulfur Protein, Journal of Biological Chemistry, vol.217, issue.43, pp.44621-44627, 2004.
DOI : 10.1016/S0014-5793(03)00981-5

S. Hasan and W. Cramer, Internal Lipid Architecture of the Hetero-Oligomeric Cytochrome b6f Complex, Structure, vol.22, issue.7, pp.1008-1015, 2014.
DOI : 10.1016/j.str.2014.05.004

A. Shapiguzov, Complex, Plant Physiology, vol.171, issue.1, pp.82-92, 2016.
DOI : 10.1104/pp.15.01893

S. Singh, Trans-membrane Signaling in Photosynthetic State Transitions, Journal of Biological Chemistry, vol.266, issue.41, pp.21740-21750, 2016.
DOI : 10.1529/biophysj.106.081372

X. Johnson, A new setup for in??vivo fluorescence imaging of photosynthetic activity, Photosynthesis Research, vol.22, issue.11, pp.85-93, 2009.
DOI : 10.1007/s11120-009-9487-2

R. Kuras and F. Wollman, The assembly of cytochrome b 6 /f complexes: An approach using genetic transformation of the green alga Chlamydomonas reinhardtii, EMBO J, vol.13, pp.1019-1027, 1994.

Y. Choquet, F. Zito, K. Wostrikoff, and F. Wollman, Cytochrome f Translation in Chlamydomonas Chloroplast Is Autoregulated by its Carboxyl-Terminal Domain, THE PLANT CELL ONLINE, vol.15, issue.>6, pp.1443-1454, 2003.
DOI : 10.1105/tpc.011692

J. Garnier, J. Maroc, and D. Guyon, Low-temperature fluorescence emission spectra and chlorophyll-protein complexes in mutants of Chlamydomonas reinhardtii: Evidence for a new chlorophyll-a-protein complex related to Photosystem I, Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol.851, issue.3, pp.395-406, 1986.
DOI : 10.1016/0005-2728(86)90076-9

D. Stroebel, Y. Choquet, J. Popot, and D. Picot, An atypical haem in the cytochrome b6f complex, Nature, vol.426, issue.6965, pp.413-418, 2003.
DOI : 10.1038/nature02155

E. Wurtz, J. Boynton, and N. Gillham, Perturbation of chloroplast DNA amounts and chloroplast gene transmission in Chlamydomonas reinhardtii by 5-fluorodeoxyuridine, Proceedings of the National Academy of Sciences, vol.74, issue.10, pp.4552-4556, 1977.
DOI : 10.1073/pnas.74.10.4552

N. Fischer, M. Hippler, P. Sétif, J. Jacquot, and J. Rochaix, The PsaC subunit of photosystem I provides an essential lysine residue for fast electron transfer to ferredoxin, The EMBO Journal, vol.17, issue.4, pp.849-858, 1998.
DOI : 10.1093/emboj/17.4.849

H. Naver, E. Boudreau, and J. Rochaix, Functional Studies of Ycf3: Its Role in Assembly of Photosystem I and Interactions with Some of Its Subunits, THE PLANT CELL ONLINE, vol.13, issue.12, pp.2731-2745, 2001.
DOI : 10.1105/tpc.13.12.2731

A. Currin, N. Swainston, P. Day, and D. Kell, Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently, Chemical Society Reviews, vol.2, issue.suppl 3, pp.1172-1239, 2015.
DOI : 10.1007/s11306-006-0037-z

J. Guo, Structure of the catalytic domain of a state transition kinase homolog from Micromonas algae, Protein & Cell, vol.18, issue.8, pp.607-619, 2013.
DOI : 10.1093/emboj/18.11.2961

S. Bergner, STATE TRANSITION7-Dependent Phosphorylation Is Modulated by Changing Environmental Conditions, and Its Absence Triggers Remodeling of Photosynthetic Protein Complexes, Plant Physiology, vol.168, issue.2, pp.615-634, 2015.
DOI : 10.1104/pp.15.00072