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Distinct functions for the two PsbP-like proteins PPL1 and PPL2 in the chloroplast thylakoid lumen of Arabidopsis.

Distinct functions for the two PsbP-like proteins PPL1 and PPL2 in the chloroplast thylakoid lumen of Arabidopsis. Research Abstract Details 

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  • Distinct functions for the two PsbP-like proteins PPL1 and PPL2 in the chloroplast thylakoid lumen of Arabidopsis. Abstract Text:

    seiko ishiharaSeiko Ishihara,atsushi takabayashiAtsushi Takabayashi,kunio idoKunio Ido,tsuyoshi endoTsuyoshi Endo,kentaro ifukuKentaro Ifuku,fumihiko satoFumihiko Sato,seiko ishiharaSeiko Ishihara,atsushi takabayashiAtsushi Takabayashi,kunio idoKunio Ido,tsuyoshi endoTsuyoshi Endo,kentaro ifukuKentaro Ifuku,fumihiko satoFumihiko Sato,seiko ishiharaSeiko Ishihara,atsushi takabayashiAtsushi Takabayashi,kunio idoKunio Ido,tsuyoshi endoTsuyoshi Endo,kentaro ifukuKentaro Ifuku,fumihiko satoFumihiko Sato,

    PsbP, an extrinsic subunit of photosystem II (PSII), is a nuclear-encoded protein that optimizes the water-splitting reaction in vivo. In addition to PsbP, higher plants have two nuclear-encoded genes for PsbP homologs (PsbP-like proteins [PPLs]) that show significant sequence similarity to a cyanobacterial PsbP homolog (cyanoP); however, the function of PPLs in higher plants has not yet been elucidated. In this study, we characterized Arabidopsis (Arabidopsis thaliana) mutants lacking either of two PPLs, PPL1 and PPL2. Phylogenetic analysis suggests that PPL1 would be an ortholog of cyanoP, and PPL2 and PsbP may have a paralogous relationship with PPL1. Analysis on mRNA expression profiles showed that PPL1 expressed under stress conditions and PPL2 coexpressed with the subunits of chloroplast NAD(P)H dehydrogenase (NDH) complex. Consistent with these suggestions, PSII activity in a ppl1 mutant was more sensitive to high-intensity light than wild type, and the recovery of photoinhibited PSII activity was delayed in ppl1 plants. Therefore, PPL1 is required for efficient repair of photodamaged PSII. Furthermore, the stoichiometric level and activity of the chloroplast NDH complex in thylakoids were severely decreased in a ppl2 mutant, demonstrating that PPL2 is a novel thylakoid lumenal factor required for accumulation of the chloroplast NDH complex. These results suggest that during endosymbiosis and subsequent gene transfer to the host nucleus, cyanoP from ancient cyanobacteria evolved into PPL1, PPL2, and PsbP, and each of them has a distinct role in photosynthetic electron transfer in Arabidopsis.

    Distinct functions for the two PsbP-like proteins PPL1 and PPL2 in the chloroplast thylakoid lumen of Arabidopsis. Publishing Authors By Initials

    s ishiharaS Ishihara,a takabayashiA Takabayashi,k idoK Ido,t endoT Endo,k ifukuK Ifuku,f satoF Sato,s ishiharaS Ishihara,a takabayashiA Takabayashi,k idoK Ido,t endoT Endo,k ifukuK Ifuku,f satoF Sato,s ishiharaS Ishihara,a takabayashiA Takabayashi,k idoK Ido,t endoT Endo,k ifukuK Ifuku,f satoF Sato,

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    Distinct functions for the two PsbP-like proteins PPL1 and PPL2 in the chloroplast thylakoid lumen of Arabidopsis. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Plant physiology

    VOLUME: 145

    Page Numbers: 668-79

    Journal Abbreviation: Plant Physiol.

    ISSN: 0032-0889

    DAY: 7

    MONTH: 09

    YEAR: 2007

    Distinct functions for the two PsbP-like proteins PPL1 and PPL2 in the chloroplast thylakoid lumen of Arabidopsis. Information

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    LANGUAGE: eng

    NlmUniqueID: 401224

    Distinct functions for the two PsbP-like proteins PPL1 and PPL2 in the chloroplast thylakoid lumen of Arabidopsis. Keywords Mesh Terms:

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    Grant and Affiliation Information for Distinct functions for the two PsbP-like proteins PPL1 and PPL2 in the chloroplast thylakoid lumen of Arabidopsis.

    AFFILIATION: Graduate School of Biostudies, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.

    Country: United States

    United States Research PublicationUnited States Research Publication

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    MEDLINETA: Plant Physiol

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