Journal Articles

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    Novel hyperthermoacidic archaeal enzymes for removal of thermophilic biofilms from stainless steel
    (Oxford University Press on behalf of Applied Microbiology International, 2023-06) Nam Y; Barnebey A; Kim HK; Yannone SM; Flint S
    AIMS: To test the efficacy of novel hot/acid hyperthermoacidic enzyme treatments on the removal of thermophilic spore-forming biofilms from stainless steel surfaces. METHODS AND RESULTS: The present study measured the efficacy of hyperthermoacidic enzymes (protease, amylase, and endoglucanase) that are optimally active at low pH (≈3.0) and high temperatures (≈80°C) at removing thermophilic bacilli biofilms from stainless steel (SS) surfaces. Plate counts, spore counts, impedance microbiology, as well as epifluorescence microscopy, and scanning electron microscopy (SEM) were used to evaluate the cleaning and sanitation of biofilms grown in a continuous flow biofilm reactor. Previously unavailable hyperthermoacidic amylase, protease, and the combination of amylase and protease were tested on Anoxybacillus flavithermus and Bacillus licheniformis, and endoglucanase was tested on Geobacillus stearothermophilus. In all cases, the heated acidic enzymatic treatments significantly reduced biofilm cells and their sheltering extracellular polymeric substances (EPS). CONCLUSIONS: Hyperthermoacidic enzymes and the associated heated acid conditions are effective at removing biofilms of thermophilic bacteria from SS surfaces that contaminate dairy plants.
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    Structural characterization of a PCP-R didomain from an archaeal nonribosomal peptide synthetase reveals novel interdomain interactions
    (Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology, 2021-02-17) Deshpande S; Altermann E; Sarojini V; Lott JS; Lee TV; Jez J
    Nonribosomal peptide synthetases (NRPSs) are multimodular enzymes that produce a wide range of bioactive peptides, such as siderophores, toxins, and antibacterial and insecticidal agents. NRPSs are dynamic proteins characterized by extensive interdomain communications as a consequence of their assembly-line mode of synthesis. Hence, crystal structures of multidomain fragments of NRPSs have aided in elucidating crucial interdomain interactions that occur during different steps of the NRPS catalytic cycle. One crucial yet unexplored interaction is that between the reductase (R) domain and the peptide carrier protein (PCP) domain. R domains are members of the short-chain dehydrogenase/reductase family and function as termination domains that catalyze the reductive release of the final peptide product from the terminal PCP domain of the NRPS. Here, we report the crystal structure of an archaeal NRPS PCP-R didomain construct. This is the first NRPS R domain structure to be determined together with the upstream PCP domain and is also the first structure of an archaeal NRPS to be reported. The structure reveals that a novel helix-turn-helix motif, found in NRPS R domains but not in other short-chain dehydrogenase/reductase family members, plays a major role in the interface between the PCP and R domains. The information derived from the described PCP-R interface will aid in gaining further mechanistic insights into the peptide termination reaction catalyzed by the R domain and may have implications in engineering NRPSs to synthesize novel peptide products.
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    Hydrogen cross-feeders of the human gastrointestinal tract.
    (Taylor & Francis Group, 2019-01-01) Smith NW; Shorten PR; Altermann EH; Roy NC; McNabb WC
    Hydrogen plays a key role in many microbial metabolic pathways in the human gastrointestinal tract (GIT) that have an impact on human nutrition, health and wellbeing. Hydrogen is produced by many members of the GIT microbiota, and may be subsequently utilized by cross-feeding microbes for growth and in the production of larger molecules. Hydrogenotrophic microbes fall into three functional groups: sulfate-reducing bacteria, methanogenic archaea and acetogenic bacteria, which can convert hydrogen into hydrogen sulfide, methane and acetate, respectively. Despite different energy yields per molecule of hydrogen used between the functional groups, all three can coexist in the human GIT. The factors affecting the numerical balance of hydrogenotrophs in the GIT remain unconfirmed. There is increasing evidence linking both hydrogen sulfide and methane to GIT diseases such as irritable bowel syndrome, and strategies for the mitigation of such health problems through targeting of hydrogenotrophs constitute an important field for further investigation.
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    Copper induces nitrification by ammonia-oxidizing bacteria and archaea in pastoral soils
    (Wiley, 12/12/2022) Matse D; Jeyakumar P; Bishop P; Anderson C
    Copper (Cu) is the main co-factor in the functioning of the ammonia monooxygenase (AMO) enzyme, which is responsible for the first step of ammonia oxidation. We report a greenhouse-based pot experiment that examines the response of ammonia-oxidizing bacteria and archaea (AOB and AOA) to different bioavailable Cu concentrations in three pastoral soils (Recent, Pallic, and Pumice soils) planted with ryegrass (Lolium perenne L.). Five treatments were used: control (no urine and Cu), urine only at 300 mg N kg-1 soil (Cu0), urine + 1 mg Cu kg-1 soil (Cu1), urine + 10 mg Cu kg-1 soil (Cu10), and urine + 100 mg Cu kg-1 soil (Cu100). Pots were destructively sampled at Day 0, 1, 7, 15, and 25 after urine application. The AOB/AOA amoA gene abundance was analyzed by real-time quantitative polymerase chain reaction at Days 1 and 15. The AOB amoA gene abundance increased 10.0- and 22.6-fold in the Recent soil and 2.1- and 2.5-fold in the Pallic soil for the Cu10 compared with Cu0 on Days 1 and 15, respectively. In contrast, the Cu100 was associated with a reduction in AOB amoA gene abundance in the Recent and Pallic soils but not in the Pumice soil. This may be due to the influence of soil cation exchange capacity differences on the bioavailable Cu. Bioavailable Cu in the Recent and Pallic soils influenced nitrification and AOB amoA gene abundance, as evidenced by the strong positive correlation between bioavailable Cu, nitrification, and AOB amoA. However, bioavailable Cu did not influence the nitrification and AOA amoA gene abundance increase.
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    Nitrification rate in dairy cattle urine patches can be inhibited by changing soil bioavailable Cu concentration
    (Elsevier, 17/01/2023) Matse D; Jeyakumar P; Bishop P; Anderson C
    Ammonia oxidation to hydroxylamine is catalyzed by the ammonia monooxygenase enzyme and copper (Cu) is a key element for this process. We investigated the effect of soil bioavailable Cu changes induced through the application of Cu-complexing compounds on nitrification rate, ammonia-oxidizing bacteria (AOB) and archaea (AOA) amoA gene abundance, and mineral nitrogen (N) leaching in urine patches using the Manawatu Recent soil. Further, evaluated the combination of organic compound calcium lignosulphonate (LS) with a growth stimulant Gibberellic acid (GA). Treatments were applied in May 2021 as late-autumn treatments: control (no urine), urine-only at 600 kg N ha-1, urine + dicyandiamide (DCD), urine + co-poly-acrylic-maleic acid (PA-MA), urine + LS, urine + split-application of LS (2LS), and urine + combination of GA plus LS (GA + LS). In addition, another four treatments were applied in July 2021 as mid-winter treatments: control, urine-only at 600 kg N ha-1, urine + GA, and urine + GA + LS. Soil bioavailable Cu and mineral N leaching were examined during the experimental period. The AOB/AOA amoA genes were quantified using quantitative polymerase chain reaction. Changes in soil bioavailable Cu across treatments correlated with nitrification rate and AOB amoA abundance in late-autumn while the AOA amoA abundance did not change. The reduction in soil bioavailable Cu induced by the PA-MA and 2LS was linked to significant (P < 0.05) reduction in mineral N leaching of 16 and 30%, respectively, relative to the urine-only. The LS did not induce a significant effect on either bioavailable Cu or mineral N leaching relative to urine-only. The GA + LS reduced mineral N leaching by 10% relative to LS in late-autumn, however, there was no significant effect in mid-winter. This study demonstrated that reducing soil bioavailable Cu can be a potential strategy to reduce N leaching from urine patches.
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    Structural characterisation of methanogen pseudomurein cell wall peptide ligases homologous to bacterial MurE/F murein peptide ligases.
    (2022-09) Subedi BP; Schofield LR; Carbone V; Wolf M; Martin WF; Ronimus RS; Sutherland-Smith AJ
    Archaea have diverse cell wall types, yet none are identical to bacterial peptidoglycan (murein). Methanogens Methanobacteria and Methanopyrus possess cell walls of pseudomurein, a structural analogue of murein. Pseudomurein differs from murein in containing the unique archaeal sugar N-acetyltalosaminuronic acid instead of N-acetylmuramic acid, β-1,3 glycosidic bonds in place of β-1,4 bonds and only l-amino acids in the peptide cross-links. We have determined crystal structures of methanogen pseudomurein peptide ligases (termed pMurE) from Methanothermus fervidus (Mfer762) and Methanothermobacter thermautotrophicus (Mth734) that are structurally most closely related to bacterial MurE peptide ligases. The homology of the archaeal pMurE and bacterial MurE enzymes is clear both in the overall structure and at the level of each of the three domains. In addition, we identified two UDP-binding sites in Mfer762 pMurE, one at the exterior surface of the interface of the N-terminal and middle domains, and a second site at an inner surface continuous with the highly conserved interface of the three domains. Residues involved in ATP binding in MurE are conserved in pMurE, suggesting that a similar ATP-binding pocket is present at the interface of the middle and the C-terminal domains of pMurE. The presence of pMurE ligases in members of the Methanobacteriales and Methanopyrales, that are structurally related to bacterial MurE ligases, supports the idea that the biosynthetic origins of archaeal pseudomurein and bacterial peptidoglycan cell walls are evolutionarily related.