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(a) Schematic diagram of transgenic lines. (b) CBB-stained SDS-PAGE gel of extracted total proteins from Arabidopsis seedlings. Western blot analysis with anti-GFP antibody (c) and anti-PHYA antibody (d). The white number above each band represents band intensity, quantified in ImageJ and normalized to RbcL, the large subunit of RuBisCO. Relative intensities to NmHO/hy1-1 for GFP (c) and to wild-type Ler for PHYA (d) are indicated. (e) Merged images of EGFP and Chl <t>fluorescence</t> in protoplasts obtained from each transgenic line.
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(a) Schematic diagram of transgenic lines. (b) CBB-stained SDS-PAGE gel of extracted total proteins from Arabidopsis seedlings. Western blot analysis with anti-GFP antibody (c) and anti-PHYA antibody (d). The white number above each band represents band intensity, quantified in ImageJ and normalized to RbcL, the large subunit of RuBisCO. Relative intensities to NmHO/hy1-1 for GFP (c) and to wild-type Ler for PHYA (d) are indicated. (e) Merged images of EGFP and Chl <t>fluorescence</t> in protoplasts obtained from each transgenic line.
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(a) Schematic diagram of transgenic lines. (b) CBB-stained SDS-PAGE gel of extracted total proteins from Arabidopsis seedlings. Western blot analysis with anti-GFP antibody (c) and anti-PHYA antibody (d). The white number above each band represents band intensity, quantified in ImageJ and normalized to RbcL, the large subunit of RuBisCO. Relative intensities to NmHO/hy1-1 for GFP (c) and to wild-type Ler for PHYA (d) are indicated. (e) Merged images of EGFP and Chl <t>fluorescence</t> in protoplasts obtained from each transgenic line.
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(a) Schematic diagram of transgenic lines. (b) CBB-stained SDS-PAGE gel of extracted total proteins from Arabidopsis seedlings. Western blot analysis with anti-GFP antibody (c) and anti-PHYA antibody (d). The white number above each band represents band intensity, quantified in ImageJ and normalized to RbcL, the large subunit of RuBisCO. Relative intensities to NmHO/hy1-1 for GFP (c) and to wild-type Ler for PHYA (d) are indicated. (e) Merged images of EGFP and Chl <t>fluorescence</t> in protoplasts obtained from each transgenic line.
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( a ) Screening the optimal vector for the yeast two-hybrid (Y2H) assay. ( b ) The interaction between p3a and TaDOF was verified by Y2H. pNubG-Fe65+pTSU2-APP was the positive control, and pNubG-Fe65+pPR3-N was the negative control. ( c ) Bimolecular <t>fluorescence</t> complementation (BiFC) confirmed that p3a and TaDOF interact in the nucleus and that they no longer interact in the absence of the zinc finger domain of TaDOF. The nuclear localization was determined with DAPI. ( d-e ) Coimmunoprecipitation (co-IP) verified that p3a and TaDOF interact in vivo ( d ) but no longer interact in the absence of the zinc finger domain of TaDOF ( e ).
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( a ) Screening the optimal vector for the yeast two-hybrid (Y2H) assay. ( b ) The interaction between p3a and TaDOF was verified by Y2H. pNubG-Fe65+pTSU2-APP was the positive control, and pNubG-Fe65+pPR3-N was the negative control. ( c ) Bimolecular <t>fluorescence</t> complementation (BiFC) confirmed that p3a and TaDOF interact in the nucleus and that they no longer interact in the absence of the zinc finger domain of TaDOF. The nuclear localization was determined with DAPI. ( d-e ) Coimmunoprecipitation (co-IP) verified that p3a and TaDOF interact in vivo ( d ) but no longer interact in the absence of the zinc finger domain of TaDOF ( e ).
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Image Search Results


(a) Schematic diagram of transgenic lines. (b) CBB-stained SDS-PAGE gel of extracted total proteins from Arabidopsis seedlings. Western blot analysis with anti-GFP antibody (c) and anti-PHYA antibody (d). The white number above each band represents band intensity, quantified in ImageJ and normalized to RbcL, the large subunit of RuBisCO. Relative intensities to NmHO/hy1-1 for GFP (c) and to wild-type Ler for PHYA (d) are indicated. (e) Merged images of EGFP and Chl fluorescence in protoplasts obtained from each transgenic line.

Journal: bioRxiv

Article Title: Introduction of regioselective bacterial heme oxygenases into Arabidopsis hy1-1 supports the retrograde heme signaling hypothesis

doi: 10.1101/2025.11.09.686882

Figure Lengend Snippet: (a) Schematic diagram of transgenic lines. (b) CBB-stained SDS-PAGE gel of extracted total proteins from Arabidopsis seedlings. Western blot analysis with anti-GFP antibody (c) and anti-PHYA antibody (d). The white number above each band represents band intensity, quantified in ImageJ and normalized to RbcL, the large subunit of RuBisCO. Relative intensities to NmHO/hy1-1 for GFP (c) and to wild-type Ler for PHYA (d) are indicated. (e) Merged images of EGFP and Chl fluorescence in protoplasts obtained from each transgenic line.

Article Snippet: GFP and Chl fluorescence signals were detected using an FV3000 confocal laser-scanning microscope (Olympus, Japan).

Techniques: Transgenic Assay, Staining, SDS Page, Western Blot, Fluorescence

( a ) Screening the optimal vector for the yeast two-hybrid (Y2H) assay. ( b ) The interaction between p3a and TaDOF was verified by Y2H. pNubG-Fe65+pTSU2-APP was the positive control, and pNubG-Fe65+pPR3-N was the negative control. ( c ) Bimolecular fluorescence complementation (BiFC) confirmed that p3a and TaDOF interact in the nucleus and that they no longer interact in the absence of the zinc finger domain of TaDOF. The nuclear localization was determined with DAPI. ( d-e ) Coimmunoprecipitation (co-IP) verified that p3a and TaDOF interact in vivo ( d ) but no longer interact in the absence of the zinc finger domain of TaDOF ( e ).

Journal: PLOS Pathogens

Article Title: A viral p3a protein targets and inhibits TaDOF transcription factors to promote the expression of susceptibility genes and facilitate viral infection

doi: 10.1371/journal.ppat.1012680

Figure Lengend Snippet: ( a ) Screening the optimal vector for the yeast two-hybrid (Y2H) assay. ( b ) The interaction between p3a and TaDOF was verified by Y2H. pNubG-Fe65+pTSU2-APP was the positive control, and pNubG-Fe65+pPR3-N was the negative control. ( c ) Bimolecular fluorescence complementation (BiFC) confirmed that p3a and TaDOF interact in the nucleus and that they no longer interact in the absence of the zinc finger domain of TaDOF. The nuclear localization was determined with DAPI. ( d-e ) Coimmunoprecipitation (co-IP) verified that p3a and TaDOF interact in vivo ( d ) but no longer interact in the absence of the zinc finger domain of TaDOF ( e ).

Article Snippet: Two days after infiltration, fluorescence signals were observed by an Olympus microscope (FV3000 Laser Scanning Confocal Microscope, Tokyo, Japan) using the following excitation wavelengths: GFP, 488 nm; mCherry, 561 nm; and chloroplast autofluorescence, 650 nm.

Techniques: Plasmid Preparation, Y2H Assay, Positive Control, Negative Control, Fluorescence, Co-Immunoprecipitation Assay, In Vivo