Enoyl-Coenzyme A Respiration via Formate Cycling in Syntrophic Bacteria

Agne, Michael; Appel, Lena; Seelmann, Carola S.; Boll, Matthias

doi:10.1128/mbio.03740-21

Cited by 5 publications

(4 citation statements)

References 57 publications

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“…Besides the absence or very low activity of the FdhAB resting state, its pronounced decrease in formate affinity is of high physiological relevance. Formate concentrations in anoxic environments are usually in the low micromolar range (~20 µM), allowing syntrophic interactions based on formate (and H2) cycling 44,45 . Thus, when in the closed resting state, FdhAB is not likely to be reduced by formate in vivo, which leaves its active site in the O2-insensitive W VI state.…”

Section: Discussionmentioning

confidence: 99%

An allosteric redox switch involved in oxygen protection in a CO2 reductase

Oliveira,

Mota,

Vilela-Alves

et al. 2023

Nat Chem Biol

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Section: Discussionmentioning

confidence: 99%

An allosteric redox switch involved in oxygen protection in a CO2 reductase

Oliveira,

Mota,

Vilela-Alves

et al. 2023

Nat Chem Biol

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“…If these NAD-dependent metabolic enzymes were acylated, however, both the upstream and downstream reactions would slow, until NAD + could be regenerated by other means. In syntrophs, NADH reoxidation by ferredoxin-independent hydrogenases or formate dehydrogenases can only proceed if H2 partial and formate levels are low and a methanogenic partner is needed to maintain these levels (Schink, 1997; Losey et al, 2017; Agne et al, 2022). Acyl-CoA dehydrogenases Swol_2126 and _2030 had increased acylation in the crotonate monocultures, suggesting that these higher acylation levels may indeed be a response to the lack of a methanogenic partner.…”

Section: Discussionmentioning

confidence: 99%

Dynamic acylome reveals metabolite driven modifications in Syntrophomonas wolfei

Muroski

Arbing

et al. 2022

Preprint

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Syntrophomonas wolfei is an anaerobic syntrophic microbe that degrades short-chain fatty acids to acetate, hydrogen, and/or formate. This thermodynamically unfavorable process proceeds through a series of reactive acyl-Coenzyme A species (RACS). In other prokaryotic and eukaryotic systems, the production of intrinsically reactive metabolites correlates with acyl-lysine modifications, which have been shown to play a significant role in metabolic processes. Analogous studies with syntrophic bacteria, however, are relatively unexplored and we hypothesize that highly abundant acylations could exist in S. wolfei proteins, corresponding to the RACS derived from degrading fatty acids. Here, by mass spectrometry-based proteomics (LC-MS/MS), we characterize and compare acylome profiles of two S. wolfei subspecies grown on different carbon substrates. Because modified S. wolfei proteins are sufficiently abundant for post-translational modification (PTM) analyses without antibody enrichment, we could identify types of acylations comprehensively, observing six types (acetyl-, butyryl-, 3-hydroxybutyryl-, crotonyl-, valeryl-, hexanyl-lysine), two of which have not been reported in any system previously. All of the acyl-PTMs identified correspond directly to RACS in fatty acid degradation pathways. A total of 369 sites of modification were identified on 237 proteins. Changing the carbon substrate altered the acylation profile. Moreover, structural studies and in vitro acylation assays of a heavily modified enzyme, acetyl-CoA transferase, provided insight on the possible impact of these acyl-protein modifications. Our findings link protein acylation by RACS to shifts in cellular metabolism.

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“…Should these NAD-dependent metabolic enzymes be acylated, however, both the upstream and downstream reactions would slow, until NAD + could be regenerated by other means. In syntrophs, NADH reoxidation by ferredoxin-independent hydrogenases or formate dehydrogenases can only proceed if H 2 partial and formate levels are low and a methanogenic partner is needed to maintain these levels ( Schink, 1997 ; Losey et al, 2017 ; Agne et al, 2022 ). Acyl-CoA dehydrogenases Swol_2126 and _2030 had increased acylation in crotonate monocultures, suggesting that higher acylation levels may indeed be a response to the lack of a methanogenic partner.…”

Section: Discussionmentioning

confidence: 99%

Dynamic acylome reveals metabolite driven modifications in Syntrophomonas wolfei

Muroski

Arbing

et al. 2022

Front. Microbiol.

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Syntrophomonas wolfei is an anaerobic syntrophic microbe that degrades short-chain fatty acids to acetate, hydrogen, and/or formate. This thermodynamically unfavorable process proceeds through a series of reactive acyl-Coenzyme A species (RACS). In other prokaryotic and eukaryotic systems, the production of intrinsically reactive metabolites correlates with acyl-lysine modifications, which have been shown to play a significant role in metabolic processes. Analogous studies with syntrophic bacteria, however, are relatively unexplored and we hypothesized that highly abundant acylations could exist in S. wolfei proteins, corresponding to the RACS derived from degrading fatty acids. Here, by mass spectrometry-based proteomics (LC–MS/MS), we characterize and compare acylome profiles of two S. wolfei subspecies grown on different carbon substrates. Because modified S. wolfei proteins are sufficiently abundant to analyze post-translational modifications (PTMs) without antibody enrichment, we could identify types of acylations comprehensively, observing six types (acetyl-, butyryl-, 3-hydroxybutyryl-, crotonyl-, valeryl-, and hexanyl-lysine), two of which have not been reported in any system previously. All of the acyl-PTMs identified correspond directly to RACS in fatty acid degradation pathways. A total of 369 sites of modification were identified on 237 proteins. Structural studies and in vitro acylation assays of a heavily modified enzyme, acetyl-CoA transferase, provided insight on the potential impact of these acyl-protein modifications. The extensive changes in acylation-type, abundance, and modification sites with carbon substrate suggest that protein acylation by RACS may be an important regulator of syntrophy.

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Enoyl-Coenzyme A Respiration via Formate Cycling in Syntrophic Bacteria

Abstract: The syntrophic interaction of fermenting bacteria and methanogenic archaea is important for the global carbon cycle. As an example, it accomplishes the conversion of biomass-derived saturated fatty acid fermentation intermediates into methane.

Cited by 5 publications

References 57 publications

An allosteric redox switch involved in oxygen protection in a CO2 reductase

An allosteric redox switch involved in oxygen protection in a CO2 reductase

Dynamic acylome reveals metabolite driven modifications in Syntrophomonas wolfei

Dynamic acylome reveals metabolite driven modifications in Syntrophomonas wolfei

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