Journal: Advanced Science

Article Title: Two Novel S ‐methyltransferases Confer Dimethylsulfide Production in Actinomycetota

doi: 10.1002/advs.202510141

Figure Lengend Snippet: Analysis of H 2 S and MeSH S ‐methylation by M . poriferae ZYF656 and its candidate Mdd enzymes. A) Simplified DMSP/DMS cycle and the key enzymes/pathways involved. Blue fonts predict enzymes/pathways in the strain M . poriferae ZYF656. B) Gas chromatography detection of DMS and MeSH produced from M . poriferae ZYF656 when incubated with 0.5 m m Met, MeSH, MMPA, H 2 S, DMSP, or a negative control. C) DMS production from E. coli BL21(DE3) with an empty vector or with clones expressing cloned mddM1 , mddM2 , when grown with 0.5 m m MeSH in M9 media. D) MeSH and DMS production from E. coli BL21(DE3) containing cloned mddM1 , mddM2 , or empty vector, when grown with 0.5 m m H 2 S in M9 media. E) RT‐qPCR analyzes of mddM1 and mddM2 in M . poriferae ZYF656 grown with 0.5 m m Met, MeSH, or H 2 S. The values for DMS and MeSH production are shown as mean ± s.d., and with three biological replicates for each strain. Significance was determined by Student's t ‐test (* p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001).

Article Snippet: To determine the functionality of MddM1 and MddM2 homologues, candidate MddM1 homologous protein sequences from Streptomyces sp. SAJ15 (A0A7M3LRJ1), Planomonospora sphaerica (A0A161LM11), Acidobacteriota bacterium (MCZ6599416.1), Acidobacteriota bacterium (MDE3069982.1), Mycolicibacterium litorale (A0A6S6P9F0), Deltaproteobacteria bacterium ( TMB00698.1 ), Dictyobacter kobayashii ( WP_126557608.1 ), Streptomyces venezuelae (F2RA35) and the MddM2 homologous protein sequence from T. bispora (D6Y5L2) were obtained from UniproKB (Table , Supporting Information), and synthesized by Sangon Biotech (Shanghai, China).

Techniques: Methylation, Gas Chromatography, Produced, Incubation, Negative Control, Plasmid Preparation, Clone Assay, Expressing, Quantitative RT-PCR

Journal: Advanced Science

Article Title: Two Novel S ‐methyltransferases Confer Dimethylsulfide Production in Actinomycetota

doi: 10.1002/advs.202510141

Figure Lengend Snippet: Maximum‐likelihood phylogenetic tree of MddM proteins. The tree was constructed using IQ‐Tree using the general time reversible model with empirical frequencies and three rates (LG + F + G4), together with the proteins previously shown to have the expected S ‐methyltransferase enzyme activity for DMS production. The scale bar indicates 0.5 amino acid substitutions per site. MddM1 and MddM2 from M. poriferae ZYF656 are highlighted by a blue star. Methyltransferase enzymes with experimentally determined Mdd activity are highlighted with a red star. The evolutionary tree uses three distinct color schemes to represent different types of information: The color blocks around the individual proteins indicate the different Mdd proteins (See Mdd protein types Key). The round dots on the branches indicate the taxonomic classification of the bacterial strains (see Taxonomy Key). The color of the leaf labels (organism names) indicates the source of the sequences (see Source Key).

Article Snippet: To determine the functionality of MddM1 and MddM2 homologues, candidate MddM1 homologous protein sequences from Streptomyces sp. SAJ15 (A0A7M3LRJ1), Planomonospora sphaerica (A0A161LM11), Acidobacteriota bacterium (MCZ6599416.1), Acidobacteriota bacterium (MDE3069982.1), Mycolicibacterium litorale (A0A6S6P9F0), Deltaproteobacteria bacterium ( TMB00698.1 ), Dictyobacter kobayashii ( WP_126557608.1 ), Streptomyces venezuelae (F2RA35) and the MddM2 homologous protein sequence from T. bispora (D6Y5L2) were obtained from UniproKB (Table , Supporting Information), and synthesized by Sangon Biotech (Shanghai, China).

Techniques: Construct, Activity Assay

Journal: Advanced Science

Article Title: Two Novel S ‐methyltransferases Confer Dimethylsulfide Production in Actinomycetota

doi: 10.1002/advs.202510141

Figure Lengend Snippet: Kinetic characterization of recombinant Tb MddM2. Effect of pH (A) and temperature (B) on the enzymatic activity of Tb MddM2. The 100% activity values were 44.73 and 58.73 nmol mg protein −1 min −1 for MeSH and H 2 S, respectively, at optimum pH, and 35.79 and 29.53 nmol mg protein −1 min −1 at optimum temperature. Substrate‐dependence of Tb MddM2 catalytic activity with varying H 2 S concentration (C), or SAM (D) when using H 2 S as a co‐substrate. Substrate‐dependence of Tb MddM2 catalytic activity with varying MeSH concentration (E), or SAM (F) when using MeSH as a co‐substrate. The kinetic parameters were obtained with 2 µg Tb MddM2 at pH 8 and 30 °C. Kinetic constants reported in the data panels were obtained by non‐linear fitting of data using the Michaelis–Menten equation as described in Figure . The values for DMS production are shown as mean ± s.d. for three biological replicates.

Article Snippet: To determine the functionality of MddM1 and MddM2 homologues, candidate MddM1 homologous protein sequences from Streptomyces sp. SAJ15 (A0A7M3LRJ1), Planomonospora sphaerica (A0A161LM11), Acidobacteriota bacterium (MCZ6599416.1), Acidobacteriota bacterium (MDE3069982.1), Mycolicibacterium litorale (A0A6S6P9F0), Deltaproteobacteria bacterium ( TMB00698.1 ), Dictyobacter kobayashii ( WP_126557608.1 ), Streptomyces venezuelae (F2RA35) and the MddM2 homologous protein sequence from T. bispora (D6Y5L2) were obtained from UniproKB (Table , Supporting Information), and synthesized by Sangon Biotech (Shanghai, China).

Techniques: Recombinant, Activity Assay, Concentration Assay

Journal: Advanced Science

Article Title: Two Novel S ‐methyltransferases Confer Dimethylsulfide Production in Actinomycetota

doi: 10.1002/advs.202510141

Figure Lengend Snippet: The impact of MddM1 and MddM2 on E. coli growth in response to H 2 S, MeSH, and oxidative stress. A) Growth of E. coli strains amended with H 2 O (control) in M9 media. B) Growth of E. coli strains with 1 m m MeSH in M9 media. C) Growth of E. coli strains with 2 m m H 2 O 2 in M9 media. D) Growth of E. coli strains with 1 m m H 2 S in M9 media. Error bars represent the standard deviation from n = 3 biological repeats.

Article Snippet: To determine the functionality of MddM1 and MddM2 homologues, candidate MddM1 homologous protein sequences from Streptomyces sp. SAJ15 (A0A7M3LRJ1), Planomonospora sphaerica (A0A161LM11), Acidobacteriota bacterium (MCZ6599416.1), Acidobacteriota bacterium (MDE3069982.1), Mycolicibacterium litorale (A0A6S6P9F0), Deltaproteobacteria bacterium ( TMB00698.1 ), Dictyobacter kobayashii ( WP_126557608.1 ), Streptomyces venezuelae (F2RA35) and the MddM2 homologous protein sequence from T. bispora (D6Y5L2) were obtained from UniproKB (Table , Supporting Information), and synthesized by Sangon Biotech (Shanghai, China).

Techniques: Control, Standard Deviation

Journal: Advanced Science

Article Title: Two Novel S ‐methyltransferases Confer Dimethylsulfide Production in Actinomycetota

doi: 10.1002/advs.202510141

Figure Lengend Snippet: Distribution of dddP and mdd genes in selected environmental metagenomic datasets. A) Relative abundance of dddP, mddH, mddA, mddM1 , and mddM2 in a sectioned Mariana Trench sediment core. B) Comparison of the relative abundance of dddP, mddH, mddA, mddM1 , and mddM2 in different environmental metagenomes. The values represent the logarithm to base 2 of their gene abundance plus 1. RA: relative abundance. The numbers of all sequences were normalized to the number of RecA sequences in each metagenome.

Article Snippet: To determine the functionality of MddM1 and MddM2 homologues, candidate MddM1 homologous protein sequences from Streptomyces sp. SAJ15 (A0A7M3LRJ1), Planomonospora sphaerica (A0A161LM11), Acidobacteriota bacterium (MCZ6599416.1), Acidobacteriota bacterium (MDE3069982.1), Mycolicibacterium litorale (A0A6S6P9F0), Deltaproteobacteria bacterium ( TMB00698.1 ), Dictyobacter kobayashii ( WP_126557608.1 ), Streptomyces venezuelae (F2RA35) and the MddM2 homologous protein sequence from T. bispora (D6Y5L2) were obtained from UniproKB (Table , Supporting Information), and synthesized by Sangon Biotech (Shanghai, China).

Techniques: Comparison

Journal: bioRxiv

Article Title: Antirrhinum flower shape: unravelling gene expression across developmental axes and boundaries

doi: 10.1101/2025.11.10.687484

Figure Lengend Snippet: Transcriptomic analysis of micro-dissected ventral petal regions of the Antirrhinum flower. (A) Heatmap with hierarchical clustering of genes identified as more expressed in the ventral petal (from dorsal vs. ventral petal comparison), based on normalised expression across the regions of the tube, palate, lip, and lobe. Normalised expression of two biological replicates is shown. Genes marked with arrows were selected for further validation. (B) Gene expression by in situ hybridisation for Antirrhinum homologues of LOG5 (top, left), RAA5a (top, right), LTPG13 (bottom, left) and SUP (bottom, right) in middle sections of A. majus flowers. Letters correspond to ventral petal (V), Dorsal petal (D), stamens (st) and carpels (ca). Scale 500 µM.

Article Snippet: It is possible that in Antirrhinum , as in Medicago , a SUP homologue extends its action to the petal whorl maintaining boundaries between different regions of the ventral petal.

Techniques: Comparison, Expressing, Biomarker Discovery, Gene Expression, In Situ, Hybridization