ApcE plays an important role in light-induced excitation energy dissipation in the Synechocystis PCC6803 phycobilisomes
Phycobilisomes (PBs) play an important role in cyanobacterial photosynthesis. They capture light and transfer excitation energy to the photosynthetic reaction centres. PBs are also central to some photoprotective and photoregulatory mechanisms that help sustain photosynthesis under non-optimal condi...
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description | Phycobilisomes (PBs) play an important role in cyanobacterial photosynthesis. They capture light and transfer excitation energy to the photosynthetic reaction centres. PBs are also central to some photoprotective and photoregulatory mechanisms that help sustain photosynthesis under non-optimal conditions. Amongst the mechanisms involved in excitation energy dissipation that are activated in response to excessive illumination is a recently discovered light-induced mechanism that is intrinsic to PBs and has been the least studied. Here, we used single-molecule spectroscopy and developed robust data analysis methods to explore the role of a terminal emitter subunit, ApcE, in this intrinsic, light-induced mechanism. We isolated the PBs from WT
Synechocystis
PCC 6803 as well as from the ApcE-C190S mutant of this strain and compared the dynamics of their fluorescence emission. PBs isolated from the mutant (i.e., ApcE-C190S-PBs), despite not binding some of the red-shifted pigments in the complex, showed similar global emission dynamics to WT-PBs. However, a detailed analysis of dynamics in the core revealed that the ApcE-C190S-PBs are less likely than WT-PBs to enter quenched states under illumination but still fully capable of doing so. This result points to an important but not exclusive role of the ApcE pigments in the light-induced intrinsic excitation energy dissipation mechanism in PBs. |
doi_str_mv | 10.1007/s11120-024-01078-6 |
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Synechocystis
PCC 6803 as well as from the ApcE-C190S mutant of this strain and compared the dynamics of their fluorescence emission. PBs isolated from the mutant (i.e., ApcE-C190S-PBs), despite not binding some of the red-shifted pigments in the complex, showed similar global emission dynamics to WT-PBs. However, a detailed analysis of dynamics in the core revealed that the ApcE-C190S-PBs are less likely than WT-PBs to enter quenched states under illumination but still fully capable of doing so. This result points to an important but not exclusive role of the ApcE pigments in the light-induced intrinsic excitation energy dissipation mechanism in PBs.</description><identifier>ISSN: 0166-8595</identifier><identifier>EISSN: 1573-5079</identifier><identifier>DOI: 10.1007/s11120-024-01078-6</identifier><identifier>PMID: 38407779</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Bacterial Proteins - metabolism ; Biochemistry ; Biomedical and Life Sciences ; energy ; Energy dissipation ; fluorescence ; Illumination ; Life Sciences ; lighting ; Mutants ; Photosynthesis ; Photosynthetic Reaction Center Complex Proteins - metabolism ; phycobilisome ; Phycobilisomes ; Phycobilisomes - metabolism ; Pigments ; Plant Genetics and Genomics ; Plant Physiology ; Plant Sciences ; radiation resistance ; Spectrometry, Fluorescence ; Spectroscopy ; Synechocystis ; Synechocystis - metabolism ; Synechocystis sp. PCC 6803</subject><ispartof>Photosynthesis research, 2024-04, Vol.160 (1), p.17-29</ispartof><rights>The Author(s) 2024</rights><rights>2024. The Author(s).</rights><rights>The Author(s) 2024. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c459t-e12527caf5f5b50bb5d9fab0e358bdc869f719b6e3880160db4df0a4deaa1edc3</cites><orcidid>0000-0002-0801-6512 ; 0000-0001-5572-5621 ; 0000-0002-4268-5517 ; 0000-0002-9033-9854 ; 0000-0002-3509-6554 ; 0000-0002-6769-0697</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11120-024-01078-6$$EPDF$$P50$$Gspringer$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11120-024-01078-6$$EHTML$$P50$$Gspringer$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,27903,27904,41467,42536,51298</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38407779$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Assefa, Gonfa Tesfaye</creatorcontrib><creatorcontrib>Botha, Joshua L.</creatorcontrib><creatorcontrib>van Heerden, Bertus</creatorcontrib><creatorcontrib>Kyeyune, Farooq</creatorcontrib><creatorcontrib>Krüger, Tjaart P. J.</creatorcontrib><creatorcontrib>Gwizdala, Michal</creatorcontrib><title>ApcE plays an important role in light-induced excitation energy dissipation in the Synechocystis PCC6803 phycobilisomes</title><title>Photosynthesis research</title><addtitle>Photosynth Res</addtitle><addtitle>Photosynth Res</addtitle><description>Phycobilisomes (PBs) play an important role in cyanobacterial photosynthesis. They capture light and transfer excitation energy to the photosynthetic reaction centres. PBs are also central to some photoprotective and photoregulatory mechanisms that help sustain photosynthesis under non-optimal conditions. Amongst the mechanisms involved in excitation energy dissipation that are activated in response to excessive illumination is a recently discovered light-induced mechanism that is intrinsic to PBs and has been the least studied. Here, we used single-molecule spectroscopy and developed robust data analysis methods to explore the role of a terminal emitter subunit, ApcE, in this intrinsic, light-induced mechanism. We isolated the PBs from WT
Synechocystis
PCC 6803 as well as from the ApcE-C190S mutant of this strain and compared the dynamics of their fluorescence emission. PBs isolated from the mutant (i.e., ApcE-C190S-PBs), despite not binding some of the red-shifted pigments in the complex, showed similar global emission dynamics to WT-PBs. However, a detailed analysis of dynamics in the core revealed that the ApcE-C190S-PBs are less likely than WT-PBs to enter quenched states under illumination but still fully capable of doing so. This result points to an important but not exclusive role of the ApcE pigments in the light-induced intrinsic excitation energy dissipation mechanism in PBs.</description><subject>Bacterial Proteins - metabolism</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>energy</subject><subject>Energy dissipation</subject><subject>fluorescence</subject><subject>Illumination</subject><subject>Life Sciences</subject><subject>lighting</subject><subject>Mutants</subject><subject>Photosynthesis</subject><subject>Photosynthetic Reaction Center Complex Proteins - metabolism</subject><subject>phycobilisome</subject><subject>Phycobilisomes</subject><subject>Phycobilisomes - metabolism</subject><subject>Pigments</subject><subject>Plant Genetics and Genomics</subject><subject>Plant Physiology</subject><subject>Plant Sciences</subject><subject>radiation resistance</subject><subject>Spectrometry, Fluorescence</subject><subject>Spectroscopy</subject><subject>Synechocystis</subject><subject>Synechocystis - metabolism</subject><subject>Synechocystis sp. 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J. ; Gwizdala, Michal</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c459t-e12527caf5f5b50bb5d9fab0e358bdc869f719b6e3880160db4df0a4deaa1edc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Bacterial Proteins - metabolism</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>energy</topic><topic>Energy dissipation</topic><topic>fluorescence</topic><topic>Illumination</topic><topic>Life Sciences</topic><topic>lighting</topic><topic>Mutants</topic><topic>Photosynthesis</topic><topic>Photosynthetic Reaction Center Complex Proteins - metabolism</topic><topic>phycobilisome</topic><topic>Phycobilisomes</topic><topic>Phycobilisomes - metabolism</topic><topic>Pigments</topic><topic>Plant Genetics and Genomics</topic><topic>Plant Physiology</topic><topic>Plant Sciences</topic><topic>radiation resistance</topic><topic>Spectrometry, Fluorescence</topic><topic>Spectroscopy</topic><topic>Synechocystis</topic><topic>Synechocystis - metabolism</topic><topic>Synechocystis sp. PCC 6803</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Assefa, Gonfa Tesfaye</creatorcontrib><creatorcontrib>Botha, Joshua L.</creatorcontrib><creatorcontrib>van Heerden, Bertus</creatorcontrib><creatorcontrib>Kyeyune, Farooq</creatorcontrib><creatorcontrib>Krüger, Tjaart P. 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J.</au><au>Gwizdala, Michal</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>ApcE plays an important role in light-induced excitation energy dissipation in the Synechocystis PCC6803 phycobilisomes</atitle><jtitle>Photosynthesis research</jtitle><stitle>Photosynth Res</stitle><addtitle>Photosynth Res</addtitle><date>2024-04-01</date><risdate>2024</risdate><volume>160</volume><issue>1</issue><spage>17</spage><epage>29</epage><pages>17-29</pages><issn>0166-8595</issn><eissn>1573-5079</eissn><abstract>Phycobilisomes (PBs) play an important role in cyanobacterial photosynthesis. They capture light and transfer excitation energy to the photosynthetic reaction centres. PBs are also central to some photoprotective and photoregulatory mechanisms that help sustain photosynthesis under non-optimal conditions. Amongst the mechanisms involved in excitation energy dissipation that are activated in response to excessive illumination is a recently discovered light-induced mechanism that is intrinsic to PBs and has been the least studied. Here, we used single-molecule spectroscopy and developed robust data analysis methods to explore the role of a terminal emitter subunit, ApcE, in this intrinsic, light-induced mechanism. We isolated the PBs from WT
Synechocystis
PCC 6803 as well as from the ApcE-C190S mutant of this strain and compared the dynamics of their fluorescence emission. PBs isolated from the mutant (i.e., ApcE-C190S-PBs), despite not binding some of the red-shifted pigments in the complex, showed similar global emission dynamics to WT-PBs. However, a detailed analysis of dynamics in the core revealed that the ApcE-C190S-PBs are less likely than WT-PBs to enter quenched states under illumination but still fully capable of doing so. This result points to an important but not exclusive role of the ApcE pigments in the light-induced intrinsic excitation energy dissipation mechanism in PBs.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>38407779</pmid><doi>10.1007/s11120-024-01078-6</doi><tpages>13</tpages><orcidid>https://orcid.org/0000-0002-0801-6512</orcidid><orcidid>https://orcid.org/0000-0001-5572-5621</orcidid><orcidid>https://orcid.org/0000-0002-4268-5517</orcidid><orcidid>https://orcid.org/0000-0002-9033-9854</orcidid><orcidid>https://orcid.org/0000-0002-3509-6554</orcidid><orcidid>https://orcid.org/0000-0002-6769-0697</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Bacterial Proteins - metabolism Biochemistry Biomedical and Life Sciences energy Energy dissipation fluorescence Illumination Life Sciences lighting Mutants Photosynthesis Photosynthetic Reaction Center Complex Proteins - metabolism phycobilisome Phycobilisomes Phycobilisomes - metabolism Pigments Plant Genetics and Genomics Plant Physiology Plant Sciences radiation resistance Spectrometry, Fluorescence Spectroscopy Synechocystis Synechocystis - metabolism Synechocystis sp. PCC 6803 |
title | ApcE plays an important role in light-induced excitation energy dissipation in the Synechocystis PCC6803 phycobilisomes |
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