Construction of protein-protein interaction network in sulfate-reducing bacteria: Unveiling of global response to Hg.

Sulfate-reducing bacteria (SRB) play pivotal roles in the biotransformation of mercury (Hg). However, unrevealed global responses of SRB to Hg have restricted our understanding of details of Hg biotransformation processes. The absence of protein-protein interaction (PPI) network under Hg stimuli has been a bottleneck of proteomic analysis for molecular mechanisms of Hg transformation. This study constructed the first comprehensive PPI network of SRB in response to Hg, encompassing 67 connected nodes, 26 independent nodes, and 121 edges, covering 93% of differentially expressed proteins from both previous studies and this study. The network suggested that proteomic changes of SRB in response to Hg occurred globally, including microbial metabolism in diverse environments, carbon metabolism, nucleic acid metabolism and translation, nucleic acid repair, transport systems, nitrogen metabolism, and methyltransferase activity, partial of which could cover the known knowledge. Antibiotic resistance was the original response revealed by this network, providing insights into of Hg biotransformation mechanisms. This study firstly provided the foundational network for a comprehensive understanding of SRB's responses to Hg, convenient for exploration of potential targets for Hg biotransformation. Furthermore, the network indicated that Hg enhances the metabolic activities and modification pathways of SRB to maintain cellular activities, shedding light on the influences of Hg on the carbon, nitrogen, and sulfur cycles at the cellular level.

Transformation of Mercuric Ions to Mercury Nanoparticles in Diatom Chaetoceros curvisetus.

Particulate HgS play crucial roles in the mercury (Hg) cycle. Approximately 20-90% of dissolved Hg can be transformed into particulate HgS by algae. However, detailed knowledge regarding these particles, including sizes and distribution, remains unknown. The present study explored the formation, distribution, and excretion of mercury nanoparticles (HgNPs) in diatom Chaetoceros curvisetus. The results demonstrated that HgNPs (HgS nanoparticles, 29.6-66.2 nm) formed intracellularly upon exposure to 5.0-100.0 µg L-1 Hg(II), accounting for 12-27% of the total Hg. HgNP concentrations significantly increased with increasing intracellular Hg(II) concentrations, while their sizes remained unaffected. HgNPs formed intracellularly and partly accumulated inside the cells (7-11%). Subsequently, the sizes of intracellular HgNPs gradually decreased to facilitate expulsion, 21-50% of which were excreted. These suggested the vital roles of HgNPs in comprehending marine Hg fate. Their unique physicochemical properties and bioavailability would influence Hg biotransformation in the ocean. Additionally, both intracellular and extracellular HgNPs contributed to Hg settling with cells, ultimately leading to Hg burial in sediments. Overall, these findings further deepened our understanding of Hg biotransformation and posed challenges in accurately estimating marine Hg flux and Hg burial.

Characterization of the mercury-binding proteins in tuna and salmon sashimi: Implications for health risk of mercury in food.

Fish consumption is one of the major ways through which humans receive exposure to mercury (Hg). The existing forms of Hg in food, particularly Hg bound to proteins, may affect the absorption of Hg by humans and subsequently its potentially toxic effects. However, the knowledge regarding Hg-binding proteins in edible fish muscle is scarce. In the present study, salmon and tuna fish muscles, collected from seven different regions and countries, were analyzed using metallomics- and proteomics-based techniques. The concentration of Hg in sashimi samples ranged from 4.4 to 317.4 ng/g. Size exclusion chromatography (SEC) coupled with inductively coupled plasma mass spectrometer (ICP-MS) showed that beta-actin was a novel Hg-binding protein from the fish muscles, and this protein could also bind bismuth (Bi), silver (Ag), and copper (Cu). Hg bound to beta-actin accounted for approximately 30.2-37.6% of the total Hg in the tuna muscles and was significantly correlated to total Hg in the fish muscles (r = 0.98, p < 0.01) and in the fraction of soluble proteins (r = 0.94, p < 0.01). These findings suggest that proteins act as the main Hg accumulation sites in edible fish; thus, increasing human exposure to Hg following gastrointestinal digestion.