Unravelling the complete genome sequence of Advenella mimigardefordensis strain DPN7T and novel insights in the catabolism of the xenobiotic polythioester precursor 3,3′-dithiodipropionate

Abstract

Advenella mimigardefordensis strain DPN7 T is a remarkable betaproteobacterium because of its extraordinary ability to use the synthetic disulfide 3,39-dithiodipropionic acid (DTDP) as the sole carbon source and electron donor for aerobic growth. One application of DTDP is as a precursor substrate for biotechnically synthesized polythioesters (PTEs), which are interesting nondegradable biopolymers applicable for plastics materials. Metabolic engineering for optimization of PTE production requires an understanding of DTDP conversion. The genome of A. mimigardefordensis strain DPN7 T was sequenced and annotated. The circular chromosome was found to be composed of 4 740 516 bp and 4112 predicted ORFs, whereas the circular plasmid consisted of 23 610 bp and 24 predicted ORFs. The genes participating in DTDP catabolism had been characterized in detail previously, but knowing the complete genome sequence and with support of Tn5 : : mob-induced mutants, putatively involved transporter proteins and a transcriptional regulator were also identified. Most probably, DTDP is transported into the cell by a specific tripartite tricarboxylate transport system and is then cleaved by the disulfide reductase LpdA, sulfoxygenated by the 3-mercaptopropionate dioxygenase Mdo, activated by the CoA ligase SucCD and desulfinated by the acyl-CoA dehydrogenase-like desulfinase AcdA. Regulation of this pathway is presumably performed by a transcriptional regulator of the xenobiotic response element family. The excessive sulfate that is inevitably produced is secreted by the cells by a unique sulfate exporter of the CPA (cation : proton antiporter) superfamily.

Structural basis for high‐affinity adipate binding to AdpC (RPA4515), an orphan periplasmic‐binding protein from the tripartite tricarboxylate transporter (TTT) family in Rhodopseudomonas palustris

“…In the study performed by Antoine et al [15], it was shown that the citrate uptake SBP BctC from B. pertussis is not only involved in citrate transport but also plays a role in gene regulation, interacting with the two-component system BctDE in order to modulate expression levels of the bctCBA system itself. The few TTT SBPs characterised so far seem to bind to substrates containing at least two or more carboxylate groups, as observed with the citrate binding TctC [33], the terephthalate-binding protein TphC [13], the disulphide 3,3 0dithiodipropionic acid (DTDP)-binding protein TctC [20] and the sulpholactate-binding protein SlcH [19], where a sulphate group gives a similar polarity to the molecule as a carboxylate group would, raising the question as to whether this would be a prevalent characteristic of this family. Although a two-component system is directly upstream of adpC on the opposite strand, bioinformatics analysis showed that the sensor domain in RPA4513, contains no transmembrane regions and encodes for a histidine kinase of the HWE family, which are soluble in the cytoplasm and are known to respond to light stimuli [30].…”

Carbohydrate uptake in Advenella mimigardefordensis strain DPN7T is mediated by periplasmic sugar oxidation and a TRAP‐transport system

“…1.1.1.100) and a putative malate/ l ‐lactate dehydrogenase (E.C. 1.1.1.27) also putatively involved in carbohydrate metabolism, are located (Wübbeler et al , ).…”

Substrate and Cofactor Range Differences of Two Cysteine Dioxygenases from Ralstonia eutropha H16

“…T (56% identical amino acids) and V. paradoxus TBEA6 (55% identical amino acids) were also found (17,18,51,52). The amino acid sequence of CdoA shared 83% identical amino acids with the type I cysteine dioxygenase from Cupriavidus pinatubonensis (formerly R. eutropha) JMP 134.…”

“…The investigated bacterial enzymes showed high specificity for cysteine, and the kinetic properties were very similar to those of the Cdo from rat, indicating that these proteins were indeed bona fide Cdos (11). During our studies on the microbial catabolism of TDP and DTDP, we identified genes coding for Cdo homologues in V. paradoxus TBEA6 (17,52), R. eutropha H16 (17), and A. mimigardefordensis DPN7 T (18,51). However, the putative Cdos from A. mimigardefordensis …”