RfpA, RfpB, and RfpC are the Master Control Elements of Far-Red Light Photoacclimation (FaRLiP)
Terrestrial cyanobacteria often occur in niches that are strongly enriched in far-red light (FRL; λ > 700 nm). Some cyanobacteria exhibit a complex and extensive photoacclimation response, known as FRL photoacclimation (FaRLiP). During the FaRLiP response, specialized paralogous proteins repl...
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Frontiers Media S.A.
2015-11-01
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Online Access: | https://www.frontiersin.org/article/10.3389/fmicb.2015.01303/full |
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author | Chi Zhao Fei Gan Gaozhong Shen Donald A. Bryant Donald A. Bryant |
author_facet | Chi Zhao Fei Gan Gaozhong Shen Donald A. Bryant Donald A. Bryant |
author_sort | Chi Zhao |
collection | DOAJ |
description | Terrestrial cyanobacteria often occur in niches that are strongly enriched in far-red light (FRL; λ > 700 nm). Some cyanobacteria exhibit a complex and extensive photoacclimation response, known as FRL photoacclimation (FaRLiP). During the FaRLiP response, specialized paralogous proteins replace 17 core subunits of the three major photosynthetic complexes: Photosystem (PS) I, PS II, and the phycobilisome. Additionally, the cells synthesize both chlorophyll (Chl) f and Chl d. Using biparental mating from Escherichia coli, we constructed null mutants of three genes, rfpA, rfpB, and rfpC, in the cyanobacteria Chlorogloeopsis fritschii PCC 9212 and Chroococcidiopsis thermalis PCC 7203. The resulting mutants were no longer able to modify their photosynthetic apparatus to absorb FRL, were no longer able to synthesize Chl f, inappropriately synthesized Chl d in white light, and were unable to transcribe genes of the FaRLiP gene cluster. We conclude that RfpA, RfpB, and RfpC constitute a FRL-activated signal transduction cascade that is the master control switch for the FaRLiP response. FRL is proposed to activate (or inactivate) the histidine kinase activity of RfpA, which leads to formation of the active state of RfpB, the key response regulator and transcription activator. RfpC may act as a phosphate shuttle between RfpA and RfpB. Our results show that reverse genetics via conjugation will be a powerful approach in detailed studies of the FaRLiP response. |
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spelling | doaj.art-90ee98fdfa2e4a64913215daceb12d992022-12-22T02:02:49ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2015-11-01610.3389/fmicb.2015.01303168681RfpA, RfpB, and RfpC are the Master Control Elements of Far-Red Light Photoacclimation (FaRLiP)Chi Zhao0Fei Gan1Gaozhong Shen2Donald A. Bryant3Donald A. Bryant4Department of Biochemistry and Molecular Biology, The Pennsylvania State UniversityUniversity Park, PA, USADepartment of Biochemistry and Molecular Biology, The Pennsylvania State UniversityUniversity Park, PA, USADepartment of Biochemistry and Molecular Biology, The Pennsylvania State UniversityUniversity Park, PA, USADepartment of Biochemistry and Molecular Biology, The Pennsylvania State UniversityUniversity Park, PA, USADepartment of Chemistry and Biochemistry, Montana State UniversityBozeman, MT, USATerrestrial cyanobacteria often occur in niches that are strongly enriched in far-red light (FRL; λ > 700 nm). Some cyanobacteria exhibit a complex and extensive photoacclimation response, known as FRL photoacclimation (FaRLiP). During the FaRLiP response, specialized paralogous proteins replace 17 core subunits of the three major photosynthetic complexes: Photosystem (PS) I, PS II, and the phycobilisome. Additionally, the cells synthesize both chlorophyll (Chl) f and Chl d. Using biparental mating from Escherichia coli, we constructed null mutants of three genes, rfpA, rfpB, and rfpC, in the cyanobacteria Chlorogloeopsis fritschii PCC 9212 and Chroococcidiopsis thermalis PCC 7203. The resulting mutants were no longer able to modify their photosynthetic apparatus to absorb FRL, were no longer able to synthesize Chl f, inappropriately synthesized Chl d in white light, and were unable to transcribe genes of the FaRLiP gene cluster. We conclude that RfpA, RfpB, and RfpC constitute a FRL-activated signal transduction cascade that is the master control switch for the FaRLiP response. FRL is proposed to activate (or inactivate) the histidine kinase activity of RfpA, which leads to formation of the active state of RfpB, the key response regulator and transcription activator. RfpC may act as a phosphate shuttle between RfpA and RfpB. Our results show that reverse genetics via conjugation will be a powerful approach in detailed studies of the FaRLiP response.https://www.frontiersin.org/article/10.3389/fmicb.2015.01303/fullphotosynthesisphotosystem Iphotosystem IIphycobilisomechlorophyll fchlorophyll d |
spellingShingle | Chi Zhao Fei Gan Gaozhong Shen Donald A. Bryant Donald A. Bryant RfpA, RfpB, and RfpC are the Master Control Elements of Far-Red Light Photoacclimation (FaRLiP) Frontiers in Microbiology photosynthesis photosystem I photosystem II phycobilisome chlorophyll f chlorophyll d |
title | RfpA, RfpB, and RfpC are the Master Control Elements of Far-Red Light Photoacclimation (FaRLiP) |
title_full | RfpA, RfpB, and RfpC are the Master Control Elements of Far-Red Light Photoacclimation (FaRLiP) |
title_fullStr | RfpA, RfpB, and RfpC are the Master Control Elements of Far-Red Light Photoacclimation (FaRLiP) |
title_full_unstemmed | RfpA, RfpB, and RfpC are the Master Control Elements of Far-Red Light Photoacclimation (FaRLiP) |
title_short | RfpA, RfpB, and RfpC are the Master Control Elements of Far-Red Light Photoacclimation (FaRLiP) |
title_sort | rfpa rfpb and rfpc are the master control elements of far red light photoacclimation farlip |
topic | photosynthesis photosystem I photosystem II phycobilisome chlorophyll f chlorophyll d |
url | https://www.frontiersin.org/article/10.3389/fmicb.2015.01303/full |
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