TY - JOUR
T1 - Extensive remodeling of the photosynthetic apparatus alters energy transfer among photosynthetic complexes when cyanobacteria acclimate to far-red light
AU - Ho, Ming Yang
AU - Niedzwiedzki, Dariusz M.
AU - MacGregor-Chatwin, Craig
AU - Gerstenecker, Gary
AU - Hunter, C. Neil
AU - Blankenship, Robert E.
AU - Bryant, Donald A.
N1 - Funding Information:
This research was conducted under the auspices of the Photosynthetic Antenna Research Center (PARC), an Energy Frontier Research Center funded by the DOE, Office of Science, Office of Basic Energy Sciences under Award Number DE-SC 0001035. This work was also supported by the National Science Foundation grant MCB-1613022 to D.A.B. Work in the laboratory of C.N.H. was supported by Advanced Award 338895 from the European Research Council which funded C.M.-C. and provided partial support for C.N.H. C.N.H. also gratefully acknowledges financial support from the Biotechnology and Biological Sciences Research Council (BBSRC UK), award number BB/M000265/1. M.-Y.H. gratefully acknowledges a travel award from PARC that allowed him to travel to Washington University in St. Louis to use the PARC spectroscopy facilities to perform the time-resolved fluorescence studies described herein. M.-Y.H. designed and performed research, analyzed and interpreted data, and wrote and edited the manuscript. D.A.B. obtained the funding for the research, directed the research, assisted in interpretation of the results, and wrote and edited the manuscript. D.M.N. performed TRF spectroscopy, analyzed and interpreted the spectroscopic data, and edited the manuscript. C.M.-C. performed the AFM studies, interpreted the results, constructed models, and prepared figures. C.N.H. provided financial support for the AFM studies, interpreted the AFM data, and assisted in preparing the figures and manuscript. G.G. performed the trypsin digestion and proteomics analysis and assist in the revision of the manuscript. R.E.B. obtained the funding for the research and contributed to the interpretation of the data and the revision of the manuscript. The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
Funding Information:
This research was conducted under the auspices of the Photosynthetic Antenna Research Center (PARC), an Energy Frontier Research Center funded by the DOE, Office of Science, Office of Basic Energy Sciences under Award Number DE-SC 0001035. This work was also supported by the National Science Foundation grant MCB-1613022 to D.A.B. Work in the laboratory of C.N.H. was supported by Advanced Award 338895 from the European Research Council which funded C.M.-C., and provided partial support for C.N.H. C.N.H. also gratefully acknowledges financial support from the Biotechnology and Biological Sciences Research Council (BBSRC UK), award number BB/M000265/1 . M.-Y.H. gratefully acknowledges a travel award from PARC that allowed him to travel to Washington University in St. Louis to use the PARC spectroscopy facilities to perform the time-resolved fluorescence studies described herein.
Publisher Copyright:
© 2019 Elsevier B.V.
PY - 2020/4/1
Y1 - 2020/4/1
N2 - Some cyanobacteria remodel their photosynthetic apparatus by a process known as Far-Red Light Photoacclimation (FaRLiP). Specific subunits of the phycobilisome (PBS), photosystem I (PSI), and photosystem II (PSII) complexes produced in visible light are replaced by paralogous subunits encoded within a conserved FaRLiP gene cluster when cells are grown in far-red light (FRL; λ = 700–800 nm). FRL-PSII complexes from the FaRLiP cyanobacterium, Synechococcus sp. PCC 7335, were purified and shown to contain Chl a, Chl d, Chl f, and pheophytin a, while FRL-PSI complexes contained only Chl a and Chl f. The spectroscopic properties of purified photosynthetic complexes from Synechococcus sp. PCC 7335 were determined individually, and energy transfer kinetics among PBS, PSII, and PSI were analyzed by time-resolved fluorescence (TRF) spectroscopy. Direct energy transfer from PSII to PSI was observed in cells (and thylakoids) grown in red light (RL), and possible routes of energy transfer in both RL- and FRL-grown cells were inferred. Three structural arrangements for RL-PSI were observed by atomic force microscopy of thylakoid membranes, but only arrays of trimeric FRL-PSI were observed in thylakoids from FRL-grown cells. Cells grown in FRL synthesized the FRL-specific complexes but also continued to synthesize some PBS and PSII complexes identical to those produced in RL. Although the light-harvesting efficiency of photosynthetic complexes produced in FRL might be lower in white light than the complexes produced in cells acclimated to white light, the FRL-complexes provide cells with the flexibility to utilize both visible and FRL to support oxygenic photosynthesis. This article is part of a Special Issue entitled Light harvesting, edited by Dr. Roberta Croce.
AB - Some cyanobacteria remodel their photosynthetic apparatus by a process known as Far-Red Light Photoacclimation (FaRLiP). Specific subunits of the phycobilisome (PBS), photosystem I (PSI), and photosystem II (PSII) complexes produced in visible light are replaced by paralogous subunits encoded within a conserved FaRLiP gene cluster when cells are grown in far-red light (FRL; λ = 700–800 nm). FRL-PSII complexes from the FaRLiP cyanobacterium, Synechococcus sp. PCC 7335, were purified and shown to contain Chl a, Chl d, Chl f, and pheophytin a, while FRL-PSI complexes contained only Chl a and Chl f. The spectroscopic properties of purified photosynthetic complexes from Synechococcus sp. PCC 7335 were determined individually, and energy transfer kinetics among PBS, PSII, and PSI were analyzed by time-resolved fluorescence (TRF) spectroscopy. Direct energy transfer from PSII to PSI was observed in cells (and thylakoids) grown in red light (RL), and possible routes of energy transfer in both RL- and FRL-grown cells were inferred. Three structural arrangements for RL-PSI were observed by atomic force microscopy of thylakoid membranes, but only arrays of trimeric FRL-PSI were observed in thylakoids from FRL-grown cells. Cells grown in FRL synthesized the FRL-specific complexes but also continued to synthesize some PBS and PSII complexes identical to those produced in RL. Although the light-harvesting efficiency of photosynthetic complexes produced in FRL might be lower in white light than the complexes produced in cells acclimated to white light, the FRL-complexes provide cells with the flexibility to utilize both visible and FRL to support oxygenic photosynthesis. This article is part of a Special Issue entitled Light harvesting, edited by Dr. Roberta Croce.
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U2 - 10.1016/j.bbabio.2019.148064
DO - 10.1016/j.bbabio.2019.148064
M3 - Article
C2 - 31421078
AN - SCOPUS:85071112081
VL - 1861
JO - Biochimica et Biophysica Acta - Bioenergetics
JF - Biochimica et Biophysica Acta - Bioenergetics
SN - 0005-2728
IS - 4
M1 - 148064
ER -