Biology subjects

Vijayanathan, M.

Publications and source records attributed to Vijayanathan, M..

4 recordsLinked to original sources

bioRxiv2025

FMO and CYP monooxygenase families determine the metabolic flux of hydroxylated tryptamine derivatives in barley (Hordum vulgare) following pathogen infection

To counteract pathogenic microorganisms, plants execute a complex resistance response that includes major metabolic reprogramming and production of bioactive defensive compounds. Barley (Hordeum vulgare) is a major cereal crop, but suffers significant yield losses due to pathogen attack every year. Here we use an untargeted metabolomic approach to assess the diversity and shifts in key barley metabolites produced in response to Pyrenophora teres f. teres infection, a hemibiotrophic fungal pathogen and causal agent of net blotch disease. Tryptophan-derived compounds, including tryptamine, serotonin, and a novel indole alkaloid - 2-oxo-tryptamine (2OT) - were among the most significantly induced and abundant compounds, with mass spectrometry imaging revealing that these metabolites accumulate at the site of infection. A transcriptomic approach identified a flavin-containing monooxygenase (FMO), which was functionally characterized as a 2-oxo-tryptamine synthase (2OTS). In addition, a cytochrome P450 (CYP71P10) was characterized as a tryptamine-5-hydroxylase, responsible for serotonin biosynthesis. These characterized genes are tightly co-expressed with genes involved in tryptophan biosynthesis and signify a major metabolic flux towards indolic compounds after infection, potentially serving as bioactive phytoalexins. Additional microbial interactions using a biotrophic fungus (Blumeria hordei; powdery mildew), a hemibiotrophic bacterium (Pseudomonas syringae), and alternative cultivars suggest that these pathways represent a generally activated resistance response in barley. These results provide new insights within the barley defense response relevant for the development of disease resistant traits in cereal crops.

plant biology↗

bioRxiv2025

The auxin gatekeepers: Evolution and diversification of the YUCCA family

The critically important YUCCA (YUC) gene family is highly conserved and specific to the plant kingdom, primarily responsible for the final and rate-limiting step for indole-3-acetic acid (IAA) biosynthesis. IAA is an essential phytohormone, involved in virtually all aspects of plant growth and development. In addition, IAA is involved in fine-tuning plant responses to biotic and abiotic interactions and stresses. While the YUC gene family has significantly expanded throughout the plant kingdom, a detailed analysis of the evolutionary patterns driving this diversification has not been performed. Here we present a comprehensive phylogenetic analysis of the YUC family, combining YUCs from species representing key evolutionary plant lineages. We identify and hierarchically classify the YUC family into six distinct classes and 41 subclasses. YUC diversity and expansion is explained in the context of protein sequence conservation, as well as spatial and gene expression patterns. The presented YUC gene landscape offers new perspectives on the distribution and evolutionary trends of this crucial family, which facilitates further YUC characterization within plant development and response to environmental change. Short summaryComprehensive phylogenetic and sequence analysis of the YUC gene family presents new insights into factors driving evolutionary diversification. HighlightsO_LIA phylogeny-based classification system for the YUCCA gene family is presented C_LIO_LIYUCCA evolution and structural diversification is described, supporting a fine-tuned spatial and temporal control of auxin biosynthesis, but also holds potential for alternative capabilities C_LI

plant biology↗

bioRxiv2022

Structural analysis unravels the functional promiscuity of Quinolone synthase-mediated polyketide biosynthesis in Aegle marmelos Correa

Quinolone synthase from Aegle marmelos (AmQNS) is a type III polyketide synthase that yields therapeutically effective quinolone and acridone compounds. Based on the high-resolution protein structure of AmQNS, this study provided a mechanistic explanation of the structure to synthetic selectivity. Additionally, it displays the comparatively wide active site entry that allows the catalytic pocket to accommodate bulky substrates, which affects the enzyme catalysis. We also develop a model framework for comprehending the structural constraints on ketide insertion, and postulate that AmQNS synthetic diversity is owing to its steric and electrostatic selectivity, which allows it to bind to a variety of core substrates. We further establish that AmQNS is structurally biased toward quinolone synthesis and only synthesizes acridone when malonyl-CoA concentrations are significantly high. In a nutshell, we anticipate that addressing the structural and molecular underpinnings of AmQNS-substrate interaction in terms of its high selectivity and specificity can aid in the development of numerous novel compounds. Besides, the approaches can also be expanded to other potential enzymes, which will help the pharmaceutical sector by expanding the pool of potential medication leads.

biochemistry↗

bioRxiv2021

Phylogenetic profiling suggests early origin of the core subunits of Polycomb Repressive Complex 2 (PRC2)

Polycomb Repressive Complex 2 (PRC2) is involved in establishing transcriptionally silent chromatin states through its ability to methylate lysine 27 of histone H3 by the catalytic subunit Enhancer of zeste [E(z)]. Polycomb group (PcG) proteins play a crucial role in the maintenance of cell identity and in developmental regulation. Previously, the diversity of PRC2 subunits within some eukaryotic lineages has been reported and its presence in early eukaryotic evolution has been hypothesized. So far however, systematic survey of the presence of PRC2 subunits in species of all eukaryotic lineages is missing. Here, we report the diversity of PRC2 core subunit proteins in different eukaryotic supergroups with emphasis on the early-diverged lineages and explore the molecular evolution of PRC2 subunits by phylogenetics. In detail, we investigate the SET-domain protein sequences and their evolution across the four domains of life and particularly focus on the structural diversity of the SET-domain subfamily containing E(z), the catalytic subunit of PRC2. We show that PRC2 subunits are already present in early eukaryotic lineages, strengthening the support for PRC2 emergence prior to diversification of eukaryotes. We identify a common presence of E(z) and ESC, suggesting that Su(z)12 may have emerged later and/or may be dispensable from the evolutionarily conserved functional core of PRC2. Furthermore, our results broaden our understanding of the E(z) evolution within the SET-domain protein family, suggesting possibilities of function evolution. Through this, we shed light on a possible emerging point of the PRC2 and the evolution of its function in eukaryotes.

evolutionary biology↗