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Biology subjects

Murphy, L. G.

Publications and source records attributed to Murphy, L. G..

2 recordsLinked to original sources

Riverine plastic litter restructures microbial vitamin B12 metabolism and generates functional heterogeneity

Rivers transport most land-derived plastic waste to the ocean, yet how this reshapes microbial metabolic potential remains poorly resolved. We characterized plastisphere and water-column communities across 14 stations along the River Rhine, integrating ATR-FTIR polymer characterization, 16S/18S rRNA amplicon profiles, and 120 metagenome-assembled genomes. Plastisphere communities were taxonomically distinct from water communities (PERMANOVA R = 0.258, p = 0.0001) and, despite no overall shift in functional centroid (R = 0.245, p = 0.125), were markedly more heterogeneous in functional composition across sites (permutest p = 0.0047). Aerobic corrin ring synthesis, the core B12 biosynthetic pathway, was among the most differentially dispersed functions and enriched on plastic at all seven paired stations (Wilcoxon exact test, W = 3, p = 0.004079). This signal coincided with a diatom-dominated eukaryotic plastisphere community; diatoms cannot synthesize B12 and depend on bacterial provisioning, linking functional and taxonomic restructuring via a plausible cross-domain mechanism. Plastisphere communities were also less tightly coupled to the river's dissolved nutrient gradient than water communities (envfit R = 0.64 vs. 0.82). Together, these results indicate that riverine plastic litter does not merely accumulate biomass passively but actively restructures specific metabolic capacities of its colonizers, exemplified by vitamin B12 metabolism.

microbiology↗

Comparison of insect and human cytochrome b561 proteins: Insights into candidate ferric reductases in insects

Cytochrome b561 (cytb561) proteins comprise a family of transmembrane oxidoreductases that transfer single electrons across a membrane. Most eukaryotic species, including insects, possess multiple cytb561 homologs. To learn more about this protein family in insects, we carried out a bioinformatics-based investigation of cytb561 family members from nine species representing eight insect orders. We performed a phylogenetic analysis to classify insect cytb561 orthologous groups. We then conducted sequence analyses and analyzed protein models to predict structural elements that may impact the biological functions and localization of these proteins, with a focus on possible ferric reductase activity. Our study revealed three orthologous groups, designated CG1275, Nemy, and CG8399, and a fourth group of less-conserved genes. We found that CG1275 and Nemy proteins are similar to a human ferric reductase, duodenal cytochrome b561 (Dcytb), and have many conserved amino acid residues that function in substrate binding in Dcytb. Notably, CG1275 and Nemy proteins contain a conserved histidine and other residues that play a role in ferric ion reduction by Dcytb. Nemy proteins were distinguished by a novel cysteine-rich cytoplasmic loop sequence. CG8399 orthologs are similar to a putative ferric reductase in humans, stromal cell-derived receptor 2. Like other members of the CYBDOM class of cytb561 proteins, these proteins contain reeler, DOMON, and cytb561 domains. Drosophila melanogaster CG8399 is the only insect cytb561 with known ferric reductase activity. Our investigation of the DOMON domain in CG8399 proteins revealed a probable heme-binding site and a possible site for ferric reduction. The fourth clade includes a group of proteins with a conserved "KXXXXKXH" non-cytoplasmic loop motif that may be a substrate binding site and is present in a potential ferric reductase, human tumor suppressor cytochrome b561. This study provides a foundation for future investigations of the biological functions of cytb561 genes in insects.

biochemistry↗