Search bioRxiv⌕ Search

bioRxiv · 10.1101/2025.02.09.637290

Complex nitrogen redox couplings control methane emissions from Arctic upland yedoma taliks

Abstract

Yedoma-permafrost holds disproportionately large carbon and nitrogen pools, concentrated in icy, Pleistocene-aged silt deposits in the Arctic. Upon thaw, these undergo microbial mineralization, releasing greenhouse gases (GHGs) including carbon-dioxide (CO2), methane (CH4) and nitrous-oxide (N2O). Here we present combined geochemical data with microbial function and community dynamics from deep-talik soil boreholes in an unsaturated yedoma upland. Our results reveal significant in-situ spatio-temporal seasonal shifts in microbial functional, community composition and diversity within 7-m deep upland talik. In situ methanogenesis persisted in the soil talik throughout the year due to the permafrost thaw. In the winter methanotrophy was negligible within and above the methanogenic zone, leading to elevated CH4 emissions to the atmosphere. This is likely due to reduced microbial methanotrophic activity, associated with lower temperatures and nitrogen availability. During summer, at and above the anoxic methanogenic zone, nitrate/nitrite mediated anaerobic oxidation of methane (N-AOM) by ANME2d and the NC-10 phylum, together with aerobic methanotrophy near the soil surface, significantly attenuated CH4 emissions. Nitrous-oxide concentrations peaked at 10 cm (7.2 {micro}M) and 105 cm (6.7 {micro}M) and were associated with denitrification and N-AOM by Methanoperedens (ANME2d). In the summer only and within the top 1 m of soil, high expression of nitrogen related genes (narG, norB, amoA, Annamox, and Feammox) indicated active redox dynamics, potentially providing nitrogen species for N-AOM. The potential N2O emissions in summer may imply higher net GHGs emission from yedoma uplands as climate warming leads to longer summers and warmer soils in the future.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Bergman, O., Eliani-Russak, E., Anthony, K. W., Sivan, O.. 2025-02-09. Complex nitrogen redox couplings control methane emissions from Arctic upland yedoma taliks. https://doi.org/10.1101/2025.02.09.637290

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

pTRIP, a novel integration plasmid for Listeria monocytogenes

In the past decades, several tools to genetically modify the human pathogen Listeria monocytogenes were developed. Here, we constructed a new integrative plasmid system for L. monocytogenes named pTRIP, for treB insertion plasmid. pTRIP is a vector which stably integrates into the treB locus of the wild type EGD-e. This locus encodes the sole trehalose-specific EIIB and EIIC component of a phosphotransferase system. Successful integration leads to the disruption of treB and thus, to an inability of the resulting L. monocytogenes strains to grow on trehalose as sole carbon source. Due to integration through double homologous recombination, it is the first integrative system which does not require antibiotic selection pressure. To assess functionality of the pTRIP system, prfA and its native promoter region were integrated into the treB locus of a {Delta}prfA strain. Complementation was confirmed in 78% of the isolated clones, indicating successful integration of prfA into the treB locus. We further constructed derivatives of pTRIP harboring the constitutive Pp60 (pTRIP1) and the inducible Prha (pTRIP2) promoter to further expand application possibilities. Microscopic analyses confirmed the functionality of both promoter constructs and showed dose-dependent induction for Prha. pTRIP is an efficient tool for stable gene expression as well as functional studies and expands genetic modification possibilities for L. monocytogenes.

microbiology↗

A rational design strategy and validation for protease-resistant fusion-inhibitor antiviral peptides

Peptide-based fusion inhibitors are promising pharmaceuticals in the fight against enveloped viruses relying on membrane fusion for host infection. However, peptide therapeutic applications have long been hindered by their poor stability in vivo. Here, we discovered that peptide inhibitors with the wildtype sequence of the heptad repeat 2 (HR2) domain of the SARS-CoV-2 spike protein are efficiently cleaved by Transmembrane Protease, Serine 2 (TMPRSS2), a key protease involved in the SARS-CoV-2 virus-cell fusion pathway. We then identified the corresponding cleavage sites and designed three protease-resistant peptides using ranking based on deep mutational scanning and natural occurrence. The three candidates all exhibit inhibitory activity in a cell-cell fusion assay. A high-resolution cryo-EM structure of the top candidate, HR2-NHN, bound to its HR1 target reveals the molecular basis for its potent activity. The top candidate of the cell-based screening assay significantly improved efficacy relative to the wildtype peptide when administered 12 h before infection in both an authentic virus-cell infection assay and a mouse assay. More broadly, our results suggest that the design strategies for protease-resistant peptides could be applied to a broad spectrum of other enveloped viruses and pave the way for the development of safe, prophylactic antivirals that can be administered before exposure.

microbiology↗

Host soluble inositol phosphate signaling promotes coronavirus replication

Coronaviruses rely extensively on host pathways for replication, making host-directed therapies an attractive strategy for broad-spectrum antivirals with reduced risk of viral resistance. Here we identify the host soluble inositol phosphate pathway as a previously unrecognized dependency for coronavirus infection. Genetic or pharmacologic inhibition of several kinases in this pathway markedly suppresses replication of both alpha- and betacoronaviruses, while increasing pathway activity promotes viral replication. We developed UNC7844, a potent multi-target inhibitor of these kinases, which reduces coronavirus replication by more than four orders of magnitude in cultured cells and suppresses coronavirus infection in mice. Mechanistically, UNC7844 suppresses inositol (pyro)phosphates production, disrupts phosphoinositide homeostasis, and impairs late endosomal dynamics, blocking early post-entry steps required for viral genome release and replication. Together, our findings establish the soluble inositol (pyro)phosphate pathway as an important regulator of coronavirus infection and highlight its inhibition as a promising host-directed antiviral strategy.

microbiology↗