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GenScript corporation a full-length plasmodium falciparum maf1 coding sequence

Few components of the TORC1 pathway remain in the P. <t>falciparum</t> genome. (A) A simplified representation of the major TOR complex 1 ( TORC1 ) components, regulators, targets, and converging pathways across several eukaryote lineages. Solid circles (●) indicate the presence of the gene coding for the component in representative members of the lineage, and hollow circles (O) indicate the absence of the corresponding component in the lineage. (B) An illustration of the generalized animal PI3K-TORC1 signaling cascade used to regulate cellular growth in the presence of amino acids and other growth factors (left) and a projection of this pathway in <t>Plasmodium</t> spp. based on the conserved components (right). Plasmodium spp. lack a class I PI3K enzyme and the other components ( PTEN , PDK , an Akt homolog containing a PH domain) typically associated with this signaling cascade. Plasmodium spp. do encode a class III PI3K enzyme (PF3D7_0515300) whose ortholog has been implicated in TORC1 signaling in human cells, as well as a PH domain lacking PKB family kinase (PF3D7_1246900) resembling human S6K . The genomes of Plasmodium parasites also encode an apparent ortholog of the TORC1 -dependent RNA polymerase III regulator <t>Maf1</t> (PF3D7_0416500).

A Full Length Plasmodium Falciparum Maf1 Coding Sequence, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Plasmodium falciparum Maf1 Confers Survival upon Amino Acid Starvation"

Article Title: Plasmodium falciparum Maf1 Confers Survival upon Amino Acid Starvation

Journal: mBio

doi: 10.1128/mBio.02317-16

Few components of the TORC1 pathway remain in the P. falciparum genome. (A) A simplified representation of the major TOR complex 1 ( TORC1 ) components, regulators, targets, and converging pathways across several eukaryote lineages. Solid circles (●) indicate the presence of the gene coding for the component in representative members of the lineage, and hollow circles (O) indicate the absence of the corresponding component in the lineage. (B) An illustration of the generalized animal PI3K-TORC1 signaling cascade used to regulate cellular growth in the presence of amino acids and other growth factors (left) and a projection of this pathway in Plasmodium spp. based on the conserved components (right). Plasmodium spp. lack a class I PI3K enzyme and the other components ( PTEN , PDK , an Akt homolog containing a PH domain) typically associated with this signaling cascade. Plasmodium spp. do encode a class III PI3K enzyme (PF3D7_0515300) whose ortholog has been implicated in TORC1 signaling in human cells, as well as a PH domain lacking PKB family kinase (PF3D7_1246900) resembling human S6K . The genomes of Plasmodium parasites also encode an apparent ortholog of the TORC1 -dependent RNA polymerase III regulator Maf1 (PF3D7_0416500).

Figure Legend Snippet: Few components of the TORC1 pathway remain in the P. falciparum genome. (A) A simplified representation of the major TOR complex 1 ( TORC1 ) components, regulators, targets, and converging pathways across several eukaryote lineages. Solid circles (●) indicate the presence of the gene coding for the component in representative members of the lineage, and hollow circles (O) indicate the absence of the corresponding component in the lineage. (B) An illustration of the generalized animal PI3K-TORC1 signaling cascade used to regulate cellular growth in the presence of amino acids and other growth factors (left) and a projection of this pathway in Plasmodium spp. based on the conserved components (right). Plasmodium spp. lack a class I PI3K enzyme and the other components ( PTEN , PDK , an Akt homolog containing a PH domain) typically associated with this signaling cascade. Plasmodium spp. do encode a class III PI3K enzyme (PF3D7_0515300) whose ortholog has been implicated in TORC1 signaling in human cells, as well as a PH domain lacking PKB family kinase (PF3D7_1246900) resembling human S6K . The genomes of Plasmodium parasites also encode an apparent ortholog of the TORC1 -dependent RNA polymerase III regulator Maf1 (PF3D7_0416500).

Techniques Used:

Functional complementation of Maf1-knockout yeast cells with a chimeric P. falciparum Maf1. (A) Schematics showing the key structural features of the yeast and Plasmodium Maf1 orthologs (Nt, N terminus; Ct, C terminus; NLS, nuclear localization signal). Vertical lines indicate the homologous region exchanged to generate the chimera for complementation. *P, known site of phosphorylation in the yeast protein. (B) Fivefold serial dilutions of from ~5,000 to ~8 yeast cells transformed with the indicated complementation vectors were plated on normal rich media or on rich media supplemented with 10 nM sirolimus, which is lethal to Maf1 knockout yeast cells. Images are representative of one of three biological replicates.

Figure Legend Snippet: Functional complementation of Maf1-knockout yeast cells with a chimeric P. falciparum Maf1. (A) Schematics showing the key structural features of the yeast and Plasmodium Maf1 orthologs (Nt, N terminus; Ct, C terminus; NLS, nuclear localization signal). Vertical lines indicate the homologous region exchanged to generate the chimera for complementation. *P, known site of phosphorylation in the yeast protein. (B) Fivefold serial dilutions of from ~5,000 to ~8 yeast cells transformed with the indicated complementation vectors were plated on normal rich media or on rich media supplemented with 10 nM sirolimus, which is lethal to Maf1 knockout yeast cells. Images are representative of one of three biological replicates.

Techniques Used: Functional Assay, Knock-Out, Phospho-proteomics, Transformation Assay

The PB-11 mutant carries a piggyBac insertion in the 5′UTR of the Maf1 gene. (A) Schematics of the Maf1 genomic locus and piggyBac insertion in wild-type and mutant parasites. Numbers below the chromosomal line indicate the reported and verified transposon insertion positions relative to the Maf1 start codon. Right-angled arrows and numbers above the chromosome line indicate the transcription start sites in wild-type (−93 nt) and PB-11 mutant (−395 nt) cells as determined by 5′-RACE. The Maf1 transcript in the PB-11 mutant arises from within the piggyBac transposon and is likely due to bidirectional promoter activity of the calmodulin promoter fragment used for drug selection in the transposon. (B) The upstream insertion site was confirmed by whole-genome sequencing (top). Coverage depth plots indicate the total number of reads mapping to each base pair around the two termini of the piggyBac insertion at the −53 TTAA site upstream of the Maf1 start codon. The maximum read coverage for each end of the transposon is indicated by the axes on the left and right (bottom). Raw reads aligned to the termini of the transposon surrounding the −53 insertion site. Each read is 100 bp in length. Colored spots indicate base mismatches within a given read and the genomic sequence.

Figure Legend Snippet: The PB-11 mutant carries a piggyBac insertion in the 5′UTR of the Maf1 gene. (A) Schematics of the Maf1 genomic locus and piggyBac insertion in wild-type and mutant parasites. Numbers below the chromosomal line indicate the reported and verified transposon insertion positions relative to the Maf1 start codon. Right-angled arrows and numbers above the chromosome line indicate the transcription start sites in wild-type (−93 nt) and PB-11 mutant (−395 nt) cells as determined by 5′-RACE. The Maf1 transcript in the PB-11 mutant arises from within the piggyBac transposon and is likely due to bidirectional promoter activity of the calmodulin promoter fragment used for drug selection in the transposon. (B) The upstream insertion site was confirmed by whole-genome sequencing (top). Coverage depth plots indicate the total number of reads mapping to each base pair around the two termini of the piggyBac insertion at the −53 TTAA site upstream of the Maf1 start codon. The maximum read coverage for each end of the transposon is indicated by the axes on the left and right (bottom). Raw reads aligned to the termini of the transposon surrounding the −53 insertion site. Each read is 100 bp in length. Colored spots indicate base mismatches within a given read and the genomic sequence.

Techniques Used: Mutagenesis, Activity Assay, Selection, Sequencing

Figure Legend Snippet: The PB-11 mutant displays an abnormal Maf1 mRNA expression profile. An analysis of the time course of Maf1 mRNA expression was performed using qRT-PCR at seven time points across the intraerythrocytic cycle and synchronous wild-type (NF54) and mutant (PB-11) parasites. Maf1 expression was quantified relative to that of the seryl-tRNA ligase transcript (PF3D7_0717700). Points represent individual biological replicates (three in total), and curves represent LOESS smoothed models fitted to the data, with the 95% confidence interval indicated by shading. ΔΔCT, threshold cycle method; hpi, hour post-red blood cell (RBC) invasion.

Techniques Used: Mutagenesis, Expressing, Quantitative RT-PCR

Maf1 mutant parasites cannot recover from a prolonged dormancy-like state induced by isoleucine starvation. Synchronous young ring-stage parasites (approximately 4 h postinvasion) were washed repeatedly and transferred to medium lacking isoleucine (Ile) for the indicated times. Recovery data denote transfer back to normal culture medium (containing isoleucine) for 72 h of growth. Parasitemia was quantified by flow cytometry. Growth was measured relative to the final level of parasitemia of a control culture incubated in normal culture medium for 72 h. P values were calculated using t tests of three biological replicates.

Figure Legend Snippet: Maf1 mutant parasites cannot recover from a prolonged dormancy-like state induced by isoleucine starvation. Synchronous young ring-stage parasites (approximately 4 h postinvasion) were washed repeatedly and transferred to medium lacking isoleucine (Ile) for the indicated times. Recovery data denote transfer back to normal culture medium (containing isoleucine) for 72 h of growth. Parasitemia was quantified by flow cytometry. Growth was measured relative to the final level of parasitemia of a control culture incubated in normal culture medium for 72 h. P values were calculated using t tests of three biological replicates.

Techniques Used: Mutagenesis, Flow Cytometry, Control, Incubation

The PB-11 mutant remains viable but loses the ability to recover within the first 72 h of starvation. (A) Parasitemia of Maf1 mutant parasites decreases more rapidly during prolonged isoleucine starvation. Synchronous young ring-stage NF54 (WT) and Maf1 insertion mutant (PB-11) parasites were washed repeatedly and transferred to medium lacking isoleucine. Samples of each parasite line were taken at 8-h intervals over the course of a 9-day (216-h) period, and parasitemia was determined by flow cytometry. Lines represent LOESS curves fitted to the data for each of three biological replicates. (B) Maf1 mutant parasites display minimal differences in death rate over the first 72 h of starvation. Regression models were fitted to the 216-h isoleucine starvation data to determine the rate of death of NF54 (WT) and Maf1 mutant (PB-11) parasites over the full 216 h or for only the first 72 h of the same data set (t 1/10 = time required to reach 1/10 the starting level of parasitemia). (C) Maf1 mutant parasites lose the ability to recover after (on average) 43 h of isoleucine starvation. Synchronous young ring-stage PB-11 parasites were washed and transferred to medium lacking isoleucine. Every 3 h, samples were transferred to normal medium for a 72-h recovery period. The final level of parasitemia after recovery was quantified by flow cytometry. A logistic regression fitted to the data shows that each hour of starvation decreases the parasitemia level to 93% of the level seen the previous hour (β o = −0.076, P < 2.00 × 10 −16 ). The logistic model fitted to the data predicts that the time point corresponding to 43 h of starvation is the point at which 50% of the PB-11 parasites are able to recover and 50% are not (t 50 ). Data shown are the results of three biological replicates.

Figure Legend Snippet: The PB-11 mutant remains viable but loses the ability to recover within the first 72 h of starvation. (A) Parasitemia of Maf1 mutant parasites decreases more rapidly during prolonged isoleucine starvation. Synchronous young ring-stage NF54 (WT) and Maf1 insertion mutant (PB-11) parasites were washed repeatedly and transferred to medium lacking isoleucine. Samples of each parasite line were taken at 8-h intervals over the course of a 9-day (216-h) period, and parasitemia was determined by flow cytometry. Lines represent LOESS curves fitted to the data for each of three biological replicates. (B) Maf1 mutant parasites display minimal differences in death rate over the first 72 h of starvation. Regression models were fitted to the 216-h isoleucine starvation data to determine the rate of death of NF54 (WT) and Maf1 mutant (PB-11) parasites over the full 216 h or for only the first 72 h of the same data set (t 1/10 = time required to reach 1/10 the starting level of parasitemia). (C) Maf1 mutant parasites lose the ability to recover after (on average) 43 h of isoleucine starvation. Synchronous young ring-stage PB-11 parasites were washed and transferred to medium lacking isoleucine. Every 3 h, samples were transferred to normal medium for a 72-h recovery period. The final level of parasitemia after recovery was quantified by flow cytometry. A logistic regression fitted to the data shows that each hour of starvation decreases the parasitemia level to 93% of the level seen the previous hour (β o = −0.076, P < 2.00 × 10 −16 ). The logistic model fitted to the data predicts that the time point corresponding to 43 h of starvation is the point at which 50% of the PB-11 parasites are able to recover and 50% are not (t 50 ). Data shown are the results of three biological replicates.

Techniques Used: Mutagenesis, Flow Cytometry

PB-11 Maf1 mutant parasites display defects in recovery from fosmidomycin exposure and low-temperature treatment. (A) Young ring-stage NF54 (WT) and Maf1 mutant (PB-11) parasites were incubated in the presence of 5 μM fosmidomycin (fosm.) for 72 h and were then “recovered” by incubation for a further 72 h in the presence of 5 μM fosmidomycin and 5 μM geranylgeraniol. Growth was measured relative to that of parasites incubated for 72 h in normal medium treated with both fosmidomycin and geranylgeraniol. (B) Young ring-stage parasites were incubated at 18°C for 72 h and were recovered by 72 h of growth at 37°C. Growth was measured relative to that of parasites incubated for 72 h at 37°C. P values were calculated using t tests of three biological replicates.

Figure Legend Snippet: PB-11 Maf1 mutant parasites display defects in recovery from fosmidomycin exposure and low-temperature treatment. (A) Young ring-stage NF54 (WT) and Maf1 mutant (PB-11) parasites were incubated in the presence of 5 μM fosmidomycin (fosm.) for 72 h and were then “recovered” by incubation for a further 72 h in the presence of 5 μM fosmidomycin and 5 μM geranylgeraniol. Growth was measured relative to that of parasites incubated for 72 h in normal medium treated with both fosmidomycin and geranylgeraniol. (B) Young ring-stage parasites were incubated at 18°C for 72 h and were recovered by 72 h of growth at 37°C. Growth was measured relative to that of parasites incubated for 72 h at 37°C. P values were calculated using t tests of three biological replicates.

Techniques Used: Mutagenesis, Incubation

PB-11 Maf1 parasites display a decreased growth rate under low-isoleucine conditions and at elevated temperatures. Growth curves were measured for NF54 (WT) and Maf1 mutant (PB-11) parasites cultured in normal culture medium at 37°C ( P < 0.0001) (A), 8 μM isoleucine (approximately 2% the concentration of normal medium) ( P < 0.001) (B), normal culture medium at 39°C ( P = 0.003) (C), and 20% (0.4 g/liter) of the glucose level of normal medium (2.0 g/liter) ( P = 0.08) (D). P values represent results of tests of the parasite line (i.e., the wild type versus PB-11) as a factor in the regression analysis. t D , doubling time.

Figure Legend Snippet: PB-11 Maf1 parasites display a decreased growth rate under low-isoleucine conditions and at elevated temperatures. Growth curves were measured for NF54 (WT) and Maf1 mutant (PB-11) parasites cultured in normal culture medium at 37°C ( P < 0.0001) (A), 8 μM isoleucine (approximately 2% the concentration of normal medium) ( P < 0.001) (B), normal culture medium at 39°C ( P = 0.003) (C), and 20% (0.4 g/liter) of the glucose level of normal medium (2.0 g/liter) ( P = 0.08) (D). P values represent results of tests of the parasite line (i.e., the wild type versus PB-11) as a factor in the regression analysis. t D , doubling time.

Techniques Used: Mutagenesis, Cell Culture, Concentration Assay

Maf1 mutant parasites display elevated pre-tRNA expression and elevated global translation under normal and isoleucine starvation conditions. (A) An alignment of the genomic pre-tRNA Tyr sequence and the mature tRNA Tyr sequence reveals an 11-nucleotide intron adjacent the anticodon. (B) Stem-loop RT-qPCR profiling of pre-tRNA expression in NF54 (WT) and Maf1 mutant (PB-11) parasites. Synchronous young ring-stage parasites were incubated in normal medium or medium lacking isoleucine for 24 h prior to RNA isolation. Pre-tRNA Tyr expression was quantified relative to 5.8S rRNA levels. (C) ELISA of puromycin incorporation relative to GAPDH (glyceraldehyde-3-phosphate dehydrogenase) gene levels in wild-type and mutant parasites under conditions of the indicated treatments. Synchronous young ring-stage parasites were incubated in normal medium or medium lacking isoleucine for 24 h prior to the 1-h puromycin pulse and subsequent harvesting. Translational arrest by cycloheximide (CHX) treatment was used as a negative control. P values were calculated using t tests of three biological replicates.

Figure Legend Snippet: Maf1 mutant parasites display elevated pre-tRNA expression and elevated global translation under normal and isoleucine starvation conditions. (A) An alignment of the genomic pre-tRNA Tyr sequence and the mature tRNA Tyr sequence reveals an 11-nucleotide intron adjacent the anticodon. (B) Stem-loop RT-qPCR profiling of pre-tRNA expression in NF54 (WT) and Maf1 mutant (PB-11) parasites. Synchronous young ring-stage parasites were incubated in normal medium or medium lacking isoleucine for 24 h prior to RNA isolation. Pre-tRNA Tyr expression was quantified relative to 5.8S rRNA levels. (C) ELISA of puromycin incorporation relative to GAPDH (glyceraldehyde-3-phosphate dehydrogenase) gene levels in wild-type and mutant parasites under conditions of the indicated treatments. Synchronous young ring-stage parasites were incubated in normal medium or medium lacking isoleucine for 24 h prior to the 1-h puromycin pulse and subsequent harvesting. Translational arrest by cycloheximide (CHX) treatment was used as a negative control. P values were calculated using t tests of three biological replicates.

Techniques Used: Mutagenesis, Expressing, Sequencing, Quantitative RT-PCR, Incubation, Isolation, Enzyme-linked Immunosorbent Assay, Negative Control

Image Search Results

Silencing of GmMEKK2 by virus‐induced gene silencing (VIGS) increased soybean mosaic virus (SMV) susceptibility. (A) Efficiency of GmMEKK2 silencing in empty vector control (EV) and GmMEKK2 ‐silenced mekk2 i1 and mekk2 i2 plants at 0, 7, 14 and 21 days post‐inoculation (dpi). (B) Phenotypes of soybean after SMV infection: EV and GmMEKK2 ‐silenced lines generated using VIGS. Images were taken at 21 dpi. (C) Disease indices of plants at 21 dpi. Lowercase letters denote statistically significant differences among groups at the same time point ( p < 0.05, one‐way ANOVA with Duncan's test). (D) Relative SMV accumulation in top new leaves of EV and GmMEKK2 ‐silenced plants at 7, 14 and 21 dpi, quantified by reverse transcription‐quantitative PCR using SMV coat protein‐specific primers.

Journal: Molecular Plant Pathology

Article Title: GmMEKK2 Disrupts the MKK1 /2– MPK4 Cascade to Amplify Immune Signalling and Confer Enhanced Resistance to Soybean Mosaic Virus

doi: 10.1111/mpp.70184

Figure Lengend Snippet: Silencing of GmMEKK2 by virus‐induced gene silencing (VIGS) increased soybean mosaic virus (SMV) susceptibility. (A) Efficiency of GmMEKK2 silencing in empty vector control (EV) and GmMEKK2 ‐silenced mekk2 i1 and mekk2 i2 plants at 0, 7, 14 and 21 days post‐inoculation (dpi). (B) Phenotypes of soybean after SMV infection: EV and GmMEKK2 ‐silenced lines generated using VIGS. Images were taken at 21 dpi. (C) Disease indices of plants at 21 dpi. Lowercase letters denote statistically significant differences among groups at the same time point ( p < 0.05, one‐way ANOVA with Duncan's test). (D) Relative SMV accumulation in top new leaves of EV and GmMEKK2 ‐silenced plants at 7, 14 and 21 dpi, quantified by reverse transcription‐quantitative PCR using SMV coat protein‐specific primers.

Article Snippet: The GmMEKK2 full‐length coding DNA sequence (CDS) was inserted into pDONOR221 (Invitrogen) and then transferred to a pB7FWG2 vector via an LR recombination reaction in the Gateway system.

Techniques: Virus, Plasmid Preparation, Control, Infection, Generated, Reverse Transcription, Real-time Polymerase Chain Reaction

Overexpression of GmMEKK2 improved soybean mosaic virus (SMV) resistance in soybean. (A) Infection symptoms on soybean leaves after SMV inoculation. NT, nontransgenic plants; ZMP1, 3, 6 and 7 indicate GmMEKK2 ‐overexpression lines 1, 3, 6 and 7, respectively. (B) Disease indices of NT and each GmMEKK2 ‐overexpression line. The disease index was investigated at 21 days post‐SMV‐inoculation. (C) Quantification of SMV content in soybean leaves. SMV‐susceptible line 1138‐2 was used as a positive control. (D) The GmMEKK2 expression pattern in NT plants after SMV inoculation. (E) Comparison of yield traits between NT and overexpression plants after SMV infection. Mock‐inoculated plants served as the control. Values labelled with different lowercase letters (a–e) are significantly different at p < 0.05 as determined by Duncan's test.

Journal: Molecular Plant Pathology

Article Title: GmMEKK2 Disrupts the MKK1 /2– MPK4 Cascade to Amplify Immune Signalling and Confer Enhanced Resistance to Soybean Mosaic Virus

doi: 10.1111/mpp.70184

Figure Lengend Snippet: Overexpression of GmMEKK2 improved soybean mosaic virus (SMV) resistance in soybean. (A) Infection symptoms on soybean leaves after SMV inoculation. NT, nontransgenic plants; ZMP1, 3, 6 and 7 indicate GmMEKK2 ‐overexpression lines 1, 3, 6 and 7, respectively. (B) Disease indices of NT and each GmMEKK2 ‐overexpression line. The disease index was investigated at 21 days post‐SMV‐inoculation. (C) Quantification of SMV content in soybean leaves. SMV‐susceptible line 1138‐2 was used as a positive control. (D) The GmMEKK2 expression pattern in NT plants after SMV inoculation. (E) Comparison of yield traits between NT and overexpression plants after SMV infection. Mock‐inoculated plants served as the control. Values labelled with different lowercase letters (a–e) are significantly different at p < 0.05 as determined by Duncan's test.

Techniques: Over Expression, Virus, Infection, Positive Control, Expressing, Comparison, Control

Expression profiles of key differentially expressed genes (DEGs) between nontransgenic (NT) and GmMEKK2 ‐overexpression lines (ZMP) involved in the reactive oxygen species (ROS)‐ and salicylic acid (SA)‐related pathways. (A) KEGG enrichment analysis of DEGs between NT and ZMP plants. Left: NT_CK versus ZMP_CK (uninfected controls); Right: NT_7d versus ZMP_7d (7 days post‐SMV‐inoculation [dpi]). Points represent enriched pathways, with size indicating gene count and colour reflecting −log 10 (adjusted p ‐value). Red arrows highlight defence‐related pathways. (B) Expression dynamics of key components among MAPK, plant hormone signalling and plant–pathogen interaction pathways. Schematic depicts signal transduction from apoplast to cytoplasm, including Ca 2+ sensors (CNGCs and CDPKs), ROS producers (Rbohs) and SA‐induced defence protein (PR1). Heatmaps show expression levels across conditions (NT and ZMP at 0, 7 and 14 dpi), with gene IDs labelled.

Journal: Molecular Plant Pathology

Article Title: GmMEKK2 Disrupts the MKK1 /2– MPK4 Cascade to Amplify Immune Signalling and Confer Enhanced Resistance to Soybean Mosaic Virus

doi: 10.1111/mpp.70184

Figure Lengend Snippet: Expression profiles of key differentially expressed genes (DEGs) between nontransgenic (NT) and GmMEKK2 ‐overexpression lines (ZMP) involved in the reactive oxygen species (ROS)‐ and salicylic acid (SA)‐related pathways. (A) KEGG enrichment analysis of DEGs between NT and ZMP plants. Left: NT_CK versus ZMP_CK (uninfected controls); Right: NT_7d versus ZMP_7d (7 days post‐SMV‐inoculation [dpi]). Points represent enriched pathways, with size indicating gene count and colour reflecting −log 10 (adjusted p ‐value). Red arrows highlight defence‐related pathways. (B) Expression dynamics of key components among MAPK, plant hormone signalling and plant–pathogen interaction pathways. Schematic depicts signal transduction from apoplast to cytoplasm, including Ca 2+ sensors (CNGCs and CDPKs), ROS producers (Rbohs) and SA‐induced defence protein (PR1). Heatmaps show expression levels across conditions (NT and ZMP at 0, 7 and 14 dpi), with gene IDs labelled.

Techniques: Expressing, Over Expression, Transduction

Kinase activity of GmMEKK2 is dispensable for its function in mediating defence signalling. (A–E) Relative expression levels of (A) GmMKK1 , (B) GmMPK4A , (C) GmMPK13‐like , (D) GmSUMM2 and (E) GmCRCK3 in nontransgenic control (NT), GmMEKK2 ‐overexpression lines (ZMP1, ZMP3 and ZMP7), empty vector control (EV) and GmMEKK2‐ silenced lines ( mekk2 i1 and mekk2 i2 ). Lowercase letters denote significant differences at p < 0.05 as determined by one‐way ANOVA with Duncan's test. (F) Domain architecture of GmMEKK2 highlighting the kinase domain (6–264 amino acids) and ATP‐binding site (K36). Autophosphorylation of GmMEKK2 was assessed by immunoblotting with α‐pSer/Thr antibody. Recombinant proteins GmMEKK1‐FLAG and GmMEKK1 K321M ‐FLAG were used as positive and negative controls, respectively. Coomassie brilliant blue staining validated the equal loading of recombinant proteins. (G) Yeast two‐hybrid analysis of GmMEKK2 interaction with GmMKK1, GmMPK4A and GmMPK13‐like. Transformants expressing pGADT7 and pGBKT7 constructs were grown on SD/−Leu/−Trp (control) and SD/−Leu/−Trp/−Ade/−His (selection) media. (H–J) Glutathione S‐transferase (GST) pull‐down assays with anti‐His and anti‐GST antibodies demonstrating direct binding between GST‐GmMEKK2 and (H) GmMKK1‐His, (I) GmMPK4A‐His and (J) GmMPK13‐like‐His.

Journal: Molecular Plant Pathology

Article Title: GmMEKK2 Disrupts the MKK1 /2– MPK4 Cascade to Amplify Immune Signalling and Confer Enhanced Resistance to Soybean Mosaic Virus

doi: 10.1111/mpp.70184

Figure Lengend Snippet: Kinase activity of GmMEKK2 is dispensable for its function in mediating defence signalling. (A–E) Relative expression levels of (A) GmMKK1 , (B) GmMPK4A , (C) GmMPK13‐like , (D) GmSUMM2 and (E) GmCRCK3 in nontransgenic control (NT), GmMEKK2 ‐overexpression lines (ZMP1, ZMP3 and ZMP7), empty vector control (EV) and GmMEKK2‐ silenced lines ( mekk2 i1 and mekk2 i2 ). Lowercase letters denote significant differences at p < 0.05 as determined by one‐way ANOVA with Duncan's test. (F) Domain architecture of GmMEKK2 highlighting the kinase domain (6–264 amino acids) and ATP‐binding site (K36). Autophosphorylation of GmMEKK2 was assessed by immunoblotting with α‐pSer/Thr antibody. Recombinant proteins GmMEKK1‐FLAG and GmMEKK1 K321M ‐FLAG were used as positive and negative controls, respectively. Coomassie brilliant blue staining validated the equal loading of recombinant proteins. (G) Yeast two‐hybrid analysis of GmMEKK2 interaction with GmMKK1, GmMPK4A and GmMPK13‐like. Transformants expressing pGADT7 and pGBKT7 constructs were grown on SD/−Leu/−Trp (control) and SD/−Leu/−Trp/−Ade/−His (selection) media. (H–J) Glutathione S‐transferase (GST) pull‐down assays with anti‐His and anti‐GST antibodies demonstrating direct binding between GST‐GmMEKK2 and (H) GmMKK1‐His, (I) GmMPK4A‐His and (J) GmMPK13‐like‐His.

Techniques: Activity Assay, Expressing, Control, Over Expression, Plasmid Preparation, Binding Assay, Western Blot, Recombinant, Staining, Construct, Selection

GmMEKK2 promotes the immune response induced by salicylic acid (SA). (A) Contents of free (SA) and bound salicylic acid (SAG) in nontransgenic (NT) and GmMEKK2 ‐overexpression (ZMP) lines. (B) GmMEKK2 expression in NT plants after exogenous hormone treatments. ETH, ethylene; ABA, abscisic acid (C–H) Expression of pivotal genes in the SA signalling pathway in NT, GmMEKK2 ‐overexpression and GmMEKK2 ‐silenced ( mekk2 i1 and mekk2 i2 ) plants at 7 days post‐inoculation. EV, empty vector. Values labelled with different lowercase letters (a–c) are significantly different at p < 0.05 as determined by Duncan's test.

Journal: Molecular Plant Pathology

Article Title: GmMEKK2 Disrupts the MKK1 /2– MPK4 Cascade to Amplify Immune Signalling and Confer Enhanced Resistance to Soybean Mosaic Virus

doi: 10.1111/mpp.70184

Figure Lengend Snippet: GmMEKK2 promotes the immune response induced by salicylic acid (SA). (A) Contents of free (SA) and bound salicylic acid (SAG) in nontransgenic (NT) and GmMEKK2 ‐overexpression (ZMP) lines. (B) GmMEKK2 expression in NT plants after exogenous hormone treatments. ETH, ethylene; ABA, abscisic acid (C–H) Expression of pivotal genes in the SA signalling pathway in NT, GmMEKK2 ‐overexpression and GmMEKK2 ‐silenced ( mekk2 i1 and mekk2 i2 ) plants at 7 days post‐inoculation. EV, empty vector. Values labelled with different lowercase letters (a–c) are significantly different at p < 0.05 as determined by Duncan's test.

Techniques: Over Expression, Expressing, Plasmid Preparation

GmMEKK2 is involved in the regulation of reactive oxygen species homeostasis in soybean. (A, B) H 2 O 2 and O 2− levels in leaves were detected at 7 days post‐inoculation (dpi) using 3,3′‐diaminobenzidine (DAB) and nitroblue tetrazolium (NBT) staining, respectively. The mock‐inoculated leaves were sampled as controls. (C–G) Trends in the gene expression of antioxidases were measured after soybean mosaic virus (SMV) infection. CK, noninoculated control (H–J) Antioxidase activities were measured. POD, peroxidase; CAT, catalase; SOD, superoxide dismutase. The statistical analysis was independently performed for GmMEKK2 ‐overexpression lines ZMP1, ZMP3 and ZMP7, and gene‐silenced lines mekk2 i1 , mekk2 i2 and nontransgenic (NT) plants at each stage. Values labelled with different lowercase letters are significantly different at p < 0.05 as determined by Duncan's test.

Journal: Molecular Plant Pathology

Article Title: GmMEKK2 Disrupts the MKK1 /2– MPK4 Cascade to Amplify Immune Signalling and Confer Enhanced Resistance to Soybean Mosaic Virus

doi: 10.1111/mpp.70184

Figure Lengend Snippet: GmMEKK2 is involved in the regulation of reactive oxygen species homeostasis in soybean. (A, B) H 2 O 2 and O 2− levels in leaves were detected at 7 days post‐inoculation (dpi) using 3,3′‐diaminobenzidine (DAB) and nitroblue tetrazolium (NBT) staining, respectively. The mock‐inoculated leaves were sampled as controls. (C–G) Trends in the gene expression of antioxidases were measured after soybean mosaic virus (SMV) infection. CK, noninoculated control (H–J) Antioxidase activities were measured. POD, peroxidase; CAT, catalase; SOD, superoxide dismutase. The statistical analysis was independently performed for GmMEKK2 ‐overexpression lines ZMP1, ZMP3 and ZMP7, and gene‐silenced lines mekk2 i1 , mekk2 i2 and nontransgenic (NT) plants at each stage. Values labelled with different lowercase letters are significantly different at p < 0.05 as determined by Duncan's test.

Techniques: Staining, Gene Expression, Virus, Infection, Control, Over Expression

Molecular mechanisms underlying the GmMEKK2‐mediated regulation of soybean mosaic virus (SMV) resistance in soybean. (A) Phenotype and regulatory mechanism of GmMEKK2 ‐overexpression plants under SMV inoculation. Left: GmMEKK2 ‐overexpression plants (ZMP) show no visible SMV symptoms with autoimmunity phenotype such as leaf yellowing. Right: In ZMP plants, GmMEKK2 (orange ellipses) interacts with GmMKK1 and GmMPK4A, blocking the phosphorylation (letter P in a blue circle) of the GmMEKK1‐GmMKK1‐GmMPK4A cascade. This inhibition represses (cross in a red circle) WRKY transcription factors and leads to non‐phosphorylated CRCK3 releasing SUMM2. This then triggers defence responses such as salicylic acid (SA)‐induced gene expression and basal reactive oxygen species (ROS) accumulation. The elevated ROS constitutivly results in autoimmunity in ZMP plants. (B) Left: Nontransgenic (NT) plants exhibit severe SMV symptoms such as mosaic leaves and mottled pods. Right: In NT plants, GmMEKK2 expression is low, so the GmMEKK1‐GmMKK1‐GmMPK4A cascade remains active. GmMPK4A phosphorylates CRCK3, which binds with and represses SUMM2. This suppresses defence responses, and leads to a ROS burst.

Journal: Molecular Plant Pathology

Article Title: GmMEKK2 Disrupts the MKK1 /2– MPK4 Cascade to Amplify Immune Signalling and Confer Enhanced Resistance to Soybean Mosaic Virus

doi: 10.1111/mpp.70184

Figure Lengend Snippet: Molecular mechanisms underlying the GmMEKK2‐mediated regulation of soybean mosaic virus (SMV) resistance in soybean. (A) Phenotype and regulatory mechanism of GmMEKK2 ‐overexpression plants under SMV inoculation. Left: GmMEKK2 ‐overexpression plants (ZMP) show no visible SMV symptoms with autoimmunity phenotype such as leaf yellowing. Right: In ZMP plants, GmMEKK2 (orange ellipses) interacts with GmMKK1 and GmMPK4A, blocking the phosphorylation (letter P in a blue circle) of the GmMEKK1‐GmMKK1‐GmMPK4A cascade. This inhibition represses (cross in a red circle) WRKY transcription factors and leads to non‐phosphorylated CRCK3 releasing SUMM2. This then triggers defence responses such as salicylic acid (SA)‐induced gene expression and basal reactive oxygen species (ROS) accumulation. The elevated ROS constitutivly results in autoimmunity in ZMP plants. (B) Left: Nontransgenic (NT) plants exhibit severe SMV symptoms such as mosaic leaves and mottled pods. Right: In NT plants, GmMEKK2 expression is low, so the GmMEKK1‐GmMKK1‐GmMPK4A cascade remains active. GmMPK4A phosphorylates CRCK3, which binds with and represses SUMM2. This suppresses defence responses, and leads to a ROS burst.

Techniques: Virus, Over Expression, Blocking Assay, Phospho-proteomics, Inhibition, Gene Expression, Expressing

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