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dc.contributor.author Poudyal, Roshan Sharma -
dc.contributor.author Rodionova, Margarita, V -
dc.contributor.author Kim, Hyunmin -
dc.contributor.author Lee, Seongsin -
dc.contributor.author Do, Eunjeong -
dc.contributor.author Allakhverdiev, Suleyman, I -
dc.contributor.author Nam, Hong Gil -
dc.contributor.author Hwang, Daehee -
dc.contributor.author Kim, Yumi -
dc.date.accessioned 2021-01-22T06:47:06Z -
dc.date.available 2021-01-22T06:47:06Z -
dc.date.created 2020-07-30 -
dc.date.issued 2020-06 -
dc.identifier.issn 2045-2322 -
dc.identifier.uri http://hdl.handle.net/20.500.11750/12599 -
dc.description.abstract A predominant physiological change that occurs during leaf senescence is a decrease in photosynthetic efficiency. An optimal organization of photosynthesis complexes in plant leaves is critical for efficient photosynthesis. However, molecular mechanisms for regulating photosynthesis complexes during leaf senescence remain largely unknown. Here we tracked photosynthesis complexes alterations during leaf senescence in Arabidopsis thaliana. Grana stack is significantly thickened and photosynthesis complexes were disassembled in senescing leaves. Defects in STN7 and CP29 led to an altered chloroplast ultrastructure and a malformation of photosynthesis complex organization in stroma lamella. Both CP29 phosphorylation by STN7 and CP29 fragmentation are highly associated with the photosynthesis complex disassembly. In turn, CP29 functions as a molecular glue to facilitate protein complex formation leading phosphorylation cascade and to maintain photosynthetic efficiency during leaf senescence. These data suggest a novel molecular mechanism to modulate leaf senescence via CP29 phosphorylation and fragmentation, serving as an efficient strategy to control photosynthesis complexes. -
dc.language English -
dc.publisher Nature Publishing Group -
dc.title Combinatory actions of CP29 phosphorylation by STN7 and stability regulate leaf age-dependent disassembly of photosynthetic complexes -
dc.type Article -
dc.identifier.doi 10.1038/s41598-020-67213-0 -
dc.identifier.scopusid 2-s2.0-85087061027 -
dc.identifier.bibliographicCitation Scientific Reports, v.10, no.1 -
dc.description.isOpenAccess TRUE -
dc.subject.keywordPlus STATE TRANSITIONS -
dc.subject.keywordPlus CHLOROPHYLL-A -
dc.subject.keywordPlus ARABIDOPSIS -
dc.subject.keywordPlus KINASE -
dc.subject.keywordPlus SENESCENCE -
dc.subject.keywordPlus LHCII -
dc.subject.keywordPlus PHOSPHOPROTEOME PROFILING REVEALS -
dc.subject.keywordPlus PHOTOSYSTEM-II -
dc.subject.keywordPlus PROTEIN-PHOSPHORYLATION -
dc.subject.keywordPlus THYLAKOID MEMBRANES -
dc.citation.number 1 -
dc.citation.title Scientific Reports -
dc.citation.volume 10 -
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Department of New Biology CBRG(Complex Biology Research Group) 1. Journal Articles

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