Project description:Sulfurospirillum multivorans is one of the few bacteria, which can anaerobically respire organohalides such as tetrachloroethene. The regulation of this organohalide respiration is in most parts unknown. Sulfurospirillum multivorans was shown to downregulate the expression of organohalide respiration-specific genes slowly when no substrate is present, over the time of approximately 100 generations. To unravel the molecular details of this peculiar regulation and the involved factors, we sequenced the primary transcriptome of the organism.

2020-10-23 | GSE139083 | GEO

uncultured Desulforhopalus sp.

Project description:uncultured Desulforhopalus sp. overview

| PRJNA1043377 | ENA

Desulforhopalus singaporensis DSM 12130

Project description:Desulforhopalus singaporensis DSM 12130

| PRJNA262255 | ENA

Proteome and acetylome of Sulfurospirillum halorespirans during long-term downregulation of organohalide respiratory genes

Project description:Organohalide respiration is an environmentally relevant type of anaerobic respiration. We show that Sulfurospirillum halorespirans undergoes the same type of downregulation of the organohalide respiratory genes as had been overserved before in S. multivorans when cultivated without chlorinated ethenes for a long period of time. We compared the proteomes and acetylomes of S. halorespirans cells cultivated in the presence of PCE with those of cells long- and short-term cultivated with nitrate as sole electron acceptor.

2018-04-05 | PXD008953 | Pride

Desulforhopalus sp. strain:52FAK

Project description:Complete genome of Desulforhopalus glucosivorans strain 52FAK

| PRJDB37753 | ENA

Identification of protein-trichloroethene interactions during organohalide respiration revealed by thermal proteome profiling

Project description:The organohalide-respiring Sulfurospirillum multivorans uses chlorinated ethenes as electron acceptors for growth under anoxic conditions. However, little is known about the interaction of these substrates with proteins. Here, we apply thermal proteome profiling (TPP) to analyze enzyme-trichloroethene interactions. TPP is commonly used to investigate protein-ligand binding through protein melting curve shifts. Several modifications in the protocol, e.g. performing the incubation under anaerobic conditions and increasing the temperature range up to 97°C, improved the detection range and allowed the investigation of oxygen-sensitive proteins. Enzymatic reductive dehalogenation was prevented by omitting the electron donor during incubations. This enabled detecting the interaction of the tetrachloroethene reductive dehalogenase PceA with trichloroethene and confirms the enzyme’s specificity for this substrate. Another 19 proteins showed significant melting curve shifts with trichloroethene, pointing to other proteins directly or indirectly interacting with trichloroethene. Interestingly, a putative response regulator reacted similarly towards trichloroethene, which is potentially in line with its proposed role in regulating trichloroethene respiration. The TPP approach is here proven to facilitate the identification of substrate-enzyme interactions of strictly anaerobic reductive dehalogenases and probably their regulators. This strategy can be used to identify yet unknown substrate specificities and potential signal-sensing proteins in other difficult to study bacteria.

2018-06-06 | PXD009308 | Pride

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