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Fig. 5 Cellular localization of the Craterostigma plantagineum glycine-rich protein 1 (CpGRP1)–GFP translational fusions. The full-length CpGRP1 coding sequence (CpGRP1-FULL-GFP) (a), the signal peptide only (CpGRP1-SP-GFP) (b) or the CpGRP1 coding sequence without the signal peptide (CpGRP1-CTERM-GFP) (c) was fused to green fluorescence protein (GFP) and transiently expressed in onion cells via particle bombardment. Images of transformed cells were taken with a confocal <t>microscope</t> after 16 h. Two representative images from different transformations are shown for each construct. Cells transformed with the full-length protein-coding sequence–GFP fusion (d) or GFP alone (e) were incubated in a 0.5 M sucrose solution for 5 min before analysing GFP fluorescence. In (d) and (e), GFP fluorescence only, bright field only or merged images are shown. Red arrows indicate plasma membranes of cells undergoing plasmolysis. Bars, 50 lm.
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Fig. 5 Cellular localization of the Craterostigma plantagineum glycine-rich protein 1 (CpGRP1)–GFP translational fusions. The full-length CpGRP1 coding sequence (CpGRP1-FULL-GFP) (a), the signal peptide only (CpGRP1-SP-GFP) (b) or the CpGRP1 coding sequence without the signal peptide (CpGRP1-CTERM-GFP) (c) was fused to green fluorescence protein (GFP) and transiently expressed in onion cells via particle bombardment. Images of transformed cells were taken with a confocal <t>microscope</t> after 16 h. Two representative images from different transformations are shown for each construct. Cells transformed with the full-length protein-coding sequence–GFP fusion (d) or GFP alone (e) were incubated in a 0.5 M sucrose solution for 5 min before analysing GFP fluorescence. In (d) and (e), GFP fluorescence only, bright field only or merged images are shown. Red arrows indicate plasma membranes of cells undergoing plasmolysis. Bars, 50 lm.
Eye Lens, supplied by Nikon, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Fig. 5 Cellular localization of the Craterostigma plantagineum glycine-rich protein 1 (CpGRP1)–GFP translational fusions. The full-length CpGRP1 coding sequence (CpGRP1-FULL-GFP) (a), the signal peptide only (CpGRP1-SP-GFP) (b) or the CpGRP1 coding sequence without the signal peptide (CpGRP1-CTERM-GFP) (c) was fused to green fluorescence protein (GFP) and transiently expressed in onion cells via particle bombardment. Images of transformed cells were taken with a confocal microscope after 16 h. Two representative images from different transformations are shown for each construct. Cells transformed with the full-length protein-coding sequence–GFP fusion (d) or GFP alone (e) were incubated in a 0.5 M sucrose solution for 5 min before analysing GFP fluorescence. In (d) and (e), GFP fluorescence only, bright field only or merged images are shown. Red arrows indicate plasma membranes of cells undergoing plasmolysis. Bars, 50 lm.

Journal: The New phytologist

Article Title: The Craterostigma plantagineum glycine-rich protein CpGRP1 interacts with a cell wall-associated protein kinase 1 (CpWAK1) and accumulates in leaf cell walls during dehydration.

doi: 10.1111/nph.13766

Figure Lengend Snippet: Fig. 5 Cellular localization of the Craterostigma plantagineum glycine-rich protein 1 (CpGRP1)–GFP translational fusions. The full-length CpGRP1 coding sequence (CpGRP1-FULL-GFP) (a), the signal peptide only (CpGRP1-SP-GFP) (b) or the CpGRP1 coding sequence without the signal peptide (CpGRP1-CTERM-GFP) (c) was fused to green fluorescence protein (GFP) and transiently expressed in onion cells via particle bombardment. Images of transformed cells were taken with a confocal microscope after 16 h. Two representative images from different transformations are shown for each construct. Cells transformed with the full-length protein-coding sequence–GFP fusion (d) or GFP alone (e) were incubated in a 0.5 M sucrose solution for 5 min before analysing GFP fluorescence. In (d) and (e), GFP fluorescence only, bright field only or merged images are shown. Red arrows indicate plasma membranes of cells undergoing plasmolysis. Bars, 50 lm.

Article Snippet: Protein fluorescence was observed using an inverted confocal laser scanning microscope (Nikon Eclipse TE2000-U/DEclipse C1; Nikon, D€usseldorf, Germany).

Techniques: Sequencing, Transformation Assay, Microscopy, Construct, Incubation, Clinical Proteomics

Fig. 6 Interaction assays in yeast and in planta. (a) Yeast interaction assays of Craterostigma plantagineum glycine-rich protein 1 (CpGRP1) with Arabidopsis thaliana cell wall-associated protein kinase 1–5 (AtWAK1–5) extracellular protein domains. (b) Interaction of A. thaliana glycine-rich protein 3 (AtGRP-3) with AtWAK1 and 2 and CpGRP1 with AtWAK2 and the cloned extracellular domain of CpWAK1 in yeast. The vector expressing the GAL4-binding domain only (pBD) was used in (b) as a replacement for AtGRP-3 or CpGRP1 to check for WAK-GAL4AD autoactivation. Yeast carrying the p53/SV40 bait–prey combination was used in (a) and (b) as a positive control for interactions. Transformed yeast cells carrying the different bait and prey combinations were resuspended in water and pipetted on synthetic minimal medium lacking tryptophan and leucine (SD-WL) or tryptophan, leucine and histidine (SD-WLH). Yeast carrying interacting protein pairs was additionally pipetted on SD-WLH plates supplemented with increasing concentrations of 3-amino-1,2,4-triazole (3-AT). Images were taken after 5 d using a scanner. (c) Interaction of CpGRP1 and CpWAK1 in planta. The C-terminal yellow fluorescence protein (YFP)-CpGRP1 and N-terminal YFP- CpWAK1 translational fusions were expressed in Nicotiana benthamiana leaves via Agrobacterium-mediated transformation. YFP fluorescence was analysed 2 d after infiltration with a confocal laser scanner microscope. Bars, 10 lm.

Journal: The New phytologist

Article Title: The Craterostigma plantagineum glycine-rich protein CpGRP1 interacts with a cell wall-associated protein kinase 1 (CpWAK1) and accumulates in leaf cell walls during dehydration.

doi: 10.1111/nph.13766

Figure Lengend Snippet: Fig. 6 Interaction assays in yeast and in planta. (a) Yeast interaction assays of Craterostigma plantagineum glycine-rich protein 1 (CpGRP1) with Arabidopsis thaliana cell wall-associated protein kinase 1–5 (AtWAK1–5) extracellular protein domains. (b) Interaction of A. thaliana glycine-rich protein 3 (AtGRP-3) with AtWAK1 and 2 and CpGRP1 with AtWAK2 and the cloned extracellular domain of CpWAK1 in yeast. The vector expressing the GAL4-binding domain only (pBD) was used in (b) as a replacement for AtGRP-3 or CpGRP1 to check for WAK-GAL4AD autoactivation. Yeast carrying the p53/SV40 bait–prey combination was used in (a) and (b) as a positive control for interactions. Transformed yeast cells carrying the different bait and prey combinations were resuspended in water and pipetted on synthetic minimal medium lacking tryptophan and leucine (SD-WL) or tryptophan, leucine and histidine (SD-WLH). Yeast carrying interacting protein pairs was additionally pipetted on SD-WLH plates supplemented with increasing concentrations of 3-amino-1,2,4-triazole (3-AT). Images were taken after 5 d using a scanner. (c) Interaction of CpGRP1 and CpWAK1 in planta. The C-terminal yellow fluorescence protein (YFP)-CpGRP1 and N-terminal YFP- CpWAK1 translational fusions were expressed in Nicotiana benthamiana leaves via Agrobacterium-mediated transformation. YFP fluorescence was analysed 2 d after infiltration with a confocal laser scanner microscope. Bars, 10 lm.

Article Snippet: Protein fluorescence was observed using an inverted confocal laser scanning microscope (Nikon Eclipse TE2000-U/DEclipse C1; Nikon, D€usseldorf, Germany).

Techniques: Clone Assay, Plasmid Preparation, Expressing, Binding Assay, Positive Control, Transformation Assay, Microscopy

Fig. 7 Analysis of the Craterostigma plantagineum cell wall-associated protein kinase (CpWAK) amino acid sequences. (a) Alignment of the CpWAK1 (GenBank accession number KT893872) and CpWAK2 (GenBank accession number KT893873) amino acid sequences deduced from the cDNA clones. Identical amino acids are indicated by asterisks, and conserved amino acids are indicated by dots or colons. Protein domains were identified using the NCBI CD-Search tool (http://www.ncbi.nlm.nih.gov/Structure/cdd/wrpsb.cgi) (Marchler-Bauer et al., 2011) and the ExPASy ScanProsite tool (http:// prosite.expasy.org/scanprosite/; de Castro et al., 2006). The N-terminal signal peptide and transmembrane domain were predicted using WoLF PSORT (http://www.genscript.com/wolf-psort.html; Horton et al., 2007) and TMHMM SERVER v.2.0 (http://www.cbs.dtu.dk/services/TMHMM/), respectively. Different domains are indicated by coloured boxes below the sequence. Red, predicted signal peptide; blue, wall-associated receptor kinase galacturonan- binding domain (pfam13947); dark green, EGF-like domain signature 2 (PS01186); light green, calcium-binding EGF-like domain signature (PS01187); orange, predicted transmembrane domain; yellow, predicted protein kinase domain (PS50011). (b) Overall amino acid conservation among CpWAK1, a putative kinase from Ricinus communis (B9RE26) and wall-associated protein kinase-like 8 (WAKL8) from Arabidopsis thaliana (Q9SA25). Identical and conserved amino acids are indicated in black and grey, respectively. (c, d) Sequence conservation (c) and hydropathy plot (d) of CpGRP1, CpWAK1 and CpWAK2 signal peptide sequences. The signal peptide cleavage site was predicted using WoLF PSORT (Horton et al., 2007) and is marked by a black triangle (c). Curves in (d) were generated according to Kyte & Doolittle (1982) using the ExPASy ProtScale tool (http://web.expasy.org/cgi-bin/protscale/ protscale.pl). (e) In vivo localization of the CpWAKs. The predicted signal peptide was fused to green fluorescence protein (GFP) and then transiently expressed in onion cells via particle bombardment. The GFP fluorescence was analysed 16 h after bombardment using a confocal microscope. Pictures of plasmolysed cells were taken 5 min after incubation in a 0.5 M sucrose solution. GFP fluorescence only, bright field only or merged images are shown (e). Red arrows indicate the cell plasma membrane undergoing plasmolysis. Bars, 50 lm.

Journal: The New phytologist

Article Title: The Craterostigma plantagineum glycine-rich protein CpGRP1 interacts with a cell wall-associated protein kinase 1 (CpWAK1) and accumulates in leaf cell walls during dehydration.

doi: 10.1111/nph.13766

Figure Lengend Snippet: Fig. 7 Analysis of the Craterostigma plantagineum cell wall-associated protein kinase (CpWAK) amino acid sequences. (a) Alignment of the CpWAK1 (GenBank accession number KT893872) and CpWAK2 (GenBank accession number KT893873) amino acid sequences deduced from the cDNA clones. Identical amino acids are indicated by asterisks, and conserved amino acids are indicated by dots or colons. Protein domains were identified using the NCBI CD-Search tool (http://www.ncbi.nlm.nih.gov/Structure/cdd/wrpsb.cgi) (Marchler-Bauer et al., 2011) and the ExPASy ScanProsite tool (http:// prosite.expasy.org/scanprosite/; de Castro et al., 2006). The N-terminal signal peptide and transmembrane domain were predicted using WoLF PSORT (http://www.genscript.com/wolf-psort.html; Horton et al., 2007) and TMHMM SERVER v.2.0 (http://www.cbs.dtu.dk/services/TMHMM/), respectively. Different domains are indicated by coloured boxes below the sequence. Red, predicted signal peptide; blue, wall-associated receptor kinase galacturonan- binding domain (pfam13947); dark green, EGF-like domain signature 2 (PS01186); light green, calcium-binding EGF-like domain signature (PS01187); orange, predicted transmembrane domain; yellow, predicted protein kinase domain (PS50011). (b) Overall amino acid conservation among CpWAK1, a putative kinase from Ricinus communis (B9RE26) and wall-associated protein kinase-like 8 (WAKL8) from Arabidopsis thaliana (Q9SA25). Identical and conserved amino acids are indicated in black and grey, respectively. (c, d) Sequence conservation (c) and hydropathy plot (d) of CpGRP1, CpWAK1 and CpWAK2 signal peptide sequences. The signal peptide cleavage site was predicted using WoLF PSORT (Horton et al., 2007) and is marked by a black triangle (c). Curves in (d) were generated according to Kyte & Doolittle (1982) using the ExPASy ProtScale tool (http://web.expasy.org/cgi-bin/protscale/ protscale.pl). (e) In vivo localization of the CpWAKs. The predicted signal peptide was fused to green fluorescence protein (GFP) and then transiently expressed in onion cells via particle bombardment. The GFP fluorescence was analysed 16 h after bombardment using a confocal microscope. Pictures of plasmolysed cells were taken 5 min after incubation in a 0.5 M sucrose solution. GFP fluorescence only, bright field only or merged images are shown (e). Red arrows indicate the cell plasma membrane undergoing plasmolysis. Bars, 50 lm.

Article Snippet: Protein fluorescence was observed using an inverted confocal laser scanning microscope (Nikon Eclipse TE2000-U/DEclipse C1; Nikon, D€usseldorf, Germany).

Techniques: Clone Assay, Sequencing, Binding Assay, Generated, In Vivo, Microscopy, Incubation, Clinical Proteomics, Membrane