Biology subjects

Gleason, A.

Publications and source records attributed to Gleason, A..

4 recordsLinked to original sources

bioRxiv2024

Seasonal patterns in b-vitamins and cobalamin co-limitation in the Northwest Atlantic

B-vitamins are important co-enzymes that have long been hypothesized to play key roles in marine ecosystems. However, environmental measurements remain scarce, which limits our understanding of their potential impact. Here, we present mass spectrometry-based measurements of b-vitamins (B1, B2, B3, B5, B6, B12) and related vitamers along a transect in the Northwest Atlantic Ocean, in both particulate phase and dissolved in seawater, seasonally over 5 years, and couple this with targeted investigations of the impact of B12 (cobalamin) on phytoplankton growth. We show that these metabolites are present at femto to pico-molar concentrations and demonstrate that season explains most variance in particulate phase b-vitamins but not dissolved, offering further evidence that metabolite inventories in these two phases are often decoupled. We find correlations between particulate organic carbon with particulate B1 and B3, and between chlorophyll a and particulate B2 and DMB in fall but not spring, indicating unique seasonal drivers of vitamin inventories. Of all measured vitamins, only cobalamin was enriched in the particulate over dissolved phase, predominantly in spring. We documented nitrogen and cobalamin co-limitation of phytoplankton growth during spring bloom decline, when dissolved cobalamin is seemingly drawn down, but not during fall, when dissolved cobalamin concentrations remain elevated. These seasonal differences may be underpinned by the increased importance of cobalamin remodeling and recycling during the fall. This study provides insights into the absolute concentrations, stoichiometry, and variability of b-vitamins in the ocean and offers evidence that cobalamin exerts seasonally-varying controls on Northwest Atlantic marine ecosystems.

microbiology↗

bioRxiv2024

Pseudocobalamin production and use in Synechococcus cultures and communities

Cobalamin influences marine microbial communities because an exogenous source is required by most eukaryotic phytoplankton, and demand can exceed supply. Pseudocobalamin is a cobalamin analog that is produced and used by most cyanobacteria but is not directly available to eukaryotic phytoplankton. Some microbes can remodel pseudocobalamin into cobalamin, but a scarcity of pseudocobalamin measurements impedes our ability to evaluate its importance for marine cobalamin production. Here, we perform simultaneous measurements of pseudocobalamin and methionine synthase (MetH), the key protein that uses it as a co-factor, in Synechococcus cultures and communities. In Synechococcus sp. WH8102, pseudocobalamin quota decreases in low temperature (17 {degrees}C) and low N:P, while MetH did not. Pseudocobalamin and MetH quotas were influenced by culture methods and growth phase. Despite the variability present in cultures, we found a comparably consistent quota of 300 {+/-} 100 pseudocobalamin molecules per cyanobacterial cell in the Northwest Atlantic Ocean, suggesting that cyanobacterial cell counts may be sufficient to estimate pseudocobalamin inventories in this region. This work offers insights into cellular pseudocobalamin metabolism, and the environmental and physiological conditions that may influence it, and provides environmental measurements to further our understanding of when and how pseudocobalamin can influence marine microbial communities.

microbiology↗

bioRxiv2023

Mouse gingival single-cell transcriptomic atlas: An activated fibroblast subpopulation guides oral barrier immunity in periodontitis

Periodontitis, one of the most common non-communicable diseases, is characterized by chronic oral inflammation and uncontrolled tooth supporting alveolar bone resorption. Its underlying mechanism to initiate aberrant oral barrier immunity has yet to be delineated. Here, we report a unique fibroblast subpopulation activated to guide oral inflammation (AG fibroblasts) identified in a single-cell RNA sequencing gingival cell atlas constructed from the mouse periodontitis models. AG fibroblasts localized beneath the gingival epithelium and in the cervical periodontal ligament responded to the ligature placement and to the discrete application of Toll-like receptor stimulants to mouse maxillary tissue. The upregulated chemokines and ligands of AG fibroblasts linked to the putative receptors of neutrophils in the early stages of periodontitis. In the established chronic inflammation, neutrophils together with AG fibroblasts appeared to induce type 3 innate lymphoid cells (ILC3s) that were the primary source of interleukin-17 cytokines. The comparative analysis of Rag2-/- and Rag2{gamma}c-/-mice suggested that ILC3 contributed to the cervical alveolar bone resorption interfacing the gingival inflammation. We propose that AG fibroblasts function as a previously unrecognized surveillant to initiate gingival inflammation leading to periodontitis through the AG fibroblast-neutrophil-ILC3 axis.

pathology↗

bioRxiv2023

Syndapin Regulates the RAP-1 GTPase to Control Endocytic Recycling via RHO-1 and Non-Muscle Myosin II

After endocytosis, many plasma membrane components are recycled via narrow-diameter membrane tubules that emerge from early endosomes to form recycling endosomes, eventually leading to their return to the plasma membrane. We previously showed that the F- BAR and SH3 domain Syndapin/PACSIN-family protein SDPN-1 is required in vivo for basolateral endocytic recycling in the C. elegans intestine. Here we sought to determine the significance of a predicted interaction between the SDPN-1 SH3 domain and a target sequence in PXF-1/PDZ- GEF1/RAPGEF2, a known exchange factor for Rap-GTPases. We found that endogenous mutations we engineered into the SDPN-1 SH3 domain, or its binding site in the PXF-1 protein, interfere with recycling in vivo, as does loss of the PXF-1 target RAP-1. Rap-GTPases have been shown in several contexts to negatively regulate RhoA activity. Our results show that RHO- 1/RhoA is enriched on SDPN-1 and RAP-1 positive endosomes in the C. elegans intestine, and loss of SDPN-1 or RAP-1 elevates RHO-1(GTP) levels on intestinal endosomes. Furthermore, we found that depletion of RHO-1 suppressed sdpn-1 mutant recycling defects, indicating that control of RHO-1 activity is a key mechanism by which SDPN-1 acts to promote endocytic recycling. RHO-1/RhoA is well-known for controlling actomyosin contraction cycles, although little is known of non-muscle myosin II on endosomes. Our analysis found that non-muscle myosin II is enriched on SDPN-1 positive endosomes, with two non-muscle myosin II heavy chain isoforms acting in apparent opposition. Depletion of nmy-2 inhibited recycling like sdpn-1 mutants, while depletion of nmy-1 suppressed sdpn-1 mutant recycling defects, indicating actomyosin contractility in controlling recycling endosome function.

cell biology↗