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Reductive debromination of polybrominated diphenyl ethers by Dehalococcoides

ABSTRACT: Extensive use of polybrominated diphenyl ethers (PBDEs) has resulted in widespread environmental distribution and concerns remain about risks to human health and ecosystems from legacy PBDE contamination. Though bioremediation has been proven to be a cost-effective and efficient technology for treating halogenated pollutants in situ, application of bioremediation technologies at PBDE-contaminated sites is restricted by a lack of knowledge about functional PBDE-dehalogenating microbes. In the current study, we observed distinct PBDE-dehalogenation activity by three previously isolated Dehalococcoides mccartyi strains (CG1, CG4, and 11a5). PBDE debromination proceeded via distinct pathways in each D. mccartyi strain and involved previously characterized (TceA11a5, PcbA1, and PcbA4) and uncharacterized (11a5_e001) reductive dehalogenases (RDase), suggesting that this phenotype may be more widespread among the Dehalococcoides than is currently recognized.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Dehalococcoides Mccartyi Dehalococcoides Mccartyi Cg1

SUBMITTER: Siyan Zhao

LAB HEAD: He Jianzhong

PROVIDER: PXD026932 | Pride | 2022-05-26

REPOSITORIES: Pride

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Project description:The strictly anaerobic bacterium Dehalococcoides mccartyi is obligatory dependent on organohalide respiration for energy conservation and growth. Due to its capability to reductively dehalogenate a multitude of toxic halogenated electron acceptors, it plays an important role in the attenuation of these compounds at respective contaminated sites. Here, D. mccartyi strain CBDB1, specialized on the dehalogenation of chloroaromatic compounds, was grown in a two-liquid phase system with 1,2,3-trichlorobenzene as electron acceptor, acetate plus CO2 as carbon source and hydrogen as electron donor. The proteome and Nε-lysine acetylome were analyzed in the lag, exponential and stationary phases. The high and almost invariable abundance of the membrane-localized organohalide respiration complex consisting of the reductive dehalogenases CbrA and CbdbA80, the uptake hydrogenase HupLS and the organohalide respiration molybdoenzyme OmeAB was shown throughout growth and also after a prolonged stationary phase. Quantification of transcripts of reductive dehalogenase genes revealed their major synthesis starting in the lag phase, which might be a prerequisite for balanced growth in the exponential phase. The analyses of the coverage of functional pathways as well as indicator analysis revealed the growth-phase specificity of the proteome, with regulatory proteins identified as important indicators for the stationary phase. The number of acetylated proteins increased from the lag to the stationary phase. We detected pronounced acetylation of key proteins of the acetate metabolism, i.e. the synthesis of acetyl-CoA and its processing via gluconeogenesis and the incomplete Wood-Ljungdahl pathway, as well as of proteins central for the biosynthesis of amino acids, co-factors and terpenoids. In addition, the partial acetylation of the reductive dehalogenases as well as of TatA, a component of the twin-arginine translocation machinery, suggests that acetylation might be directly involved in the maintenance of the organohalide respiration capacity of D. mccartyi over periods without access to halogenated electron acceptors.

			Action	DRS
	11a5-1.raw	Raw
	11a5-2.raw	Raw
	11a5-uniprot-proteome_UP000076394.fasta	Fasta
	A_11a5.msf	Msf
	A_11a5.msfView	Msf

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Reductive debromination of polybrominated diphenyl ethers by Dehalococcoides

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