Differentiation of the multiple S- and N-oxide-reducing activities ofEscherichia coli

Damaraju, Sambasivarao; Weiner, Joël H.

doi:10.1007/bf02092258

Cited by 17 publications

(12 citation statements)

References 24 publications

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“…Me 2 SO reductase activity was monitored by the oxidation of reduced benzyl viologen by the substrate TMAO. Fumarate reductase activity was monitored in an assay system similar to the Me 2 SO reductase, except fumarate was used as a substrate (22,30).…”

Section: Methodsmentioning

confidence: 99%

Investigation of Escherichia coli Dimethyl Sulfoxide Reductase Assembly and Processing in Strains Defective for the sec-Independent Protein Translocation System Membrane Targeting and Translocation

Damaraju

Dawson

Zhang

et al. 2001

Journal of Biological Chemistry

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Dimethyl sulfoxide reductase is a heterotrimeric enzyme (DmsABC) localized to the cytoplasmic surface of the inner membrane. Targeting of the DmsA and DmsB catalytic subunits to the membrane requires the membrane targeting and translocation (Mtt) system. The DmsAB dimer is a member of a family of extrinsic, cytoplasmic facing membrane subunits that require Mtt in order to assemble on the membrane. We show that the MttA 2 , MttB, and presumably MttA 1 but not the MttC proteins are required for targeting DmsAB to the membrane. Unlike other Mtt substrates such as trimethylamine N-oxide reductase, the soluble cytoplasmic DmsAB dimer that accumulates in the mtt deletions is very labile. Deletion of the mttA 2 or mttB genes also prevents anaerobic growth on fumarate even though fumarate reductase does not require Mtt for assembly. This was due to the lethality of membrane insertion of DmsC in the absence of the DmsAB subunits. In the absence of DmsC, DmsAB accumulates in the cytoplasm. A 45-amino acid leader on DmsA is removed during assembly. Processing does not require DmsC but does require Mtt. Translocation of DmsAB to the periplasm is not required for processing. The leader may be cleaved by a novel leader peptidase, or the long DmsA leader may traverse the membrane through the Mtt system resulting in cleavage by the periplasmic leader peptidase I followed by release of DmsA into the cytoplasm.

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Section: Methodsmentioning

confidence: 99%

Investigation of Escherichia coli Dimethyl Sulfoxide Reductase Assembly and Processing in Strains Defective for the sec-Independent Protein Translocation System Membrane Targeting and Translocation

Damaraju

Dawson

Zhang

et al. 2001

Journal of Biological Chemistry

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“…Respiratory growth of E. coli on several S-and N-oxides has been established, and these studies have demonstrated that the terminal reductases DmsABC and trimethylamine N-oxide (TMAO) reductase (TorA) play important roles in this process (Sambasivarao & Weiner, 1991a). While only DmsABC is responsible for anaerobic growth on DMSO, both DmsABC and TorA are responsible for anaerobic growth on TMAO (Sambasivarao & Weiner, 1991a).…”

Section: Introductionmentioning

confidence: 99%

“…While only DmsABC is responsible for anaerobic growth on DMSO, both DmsABC and TorA are responsible for anaerobic growth on TMAO (Sambasivarao & Weiner, 1991a). The molybdoenzyme TorA (Mejean et al, 1994;Yamamoto et al, 1986) is inducible (Pascal et al, 1984;Silvestro et al, 1988) and periplasmic (Silvestro e t al., 1989).…”

Section: Introductionmentioning

confidence: 99%

“…Strains and plasmids. E. coli strains used in this study were: HBlOl [s~pE44 ksdS20 Z(r;m;) recA73 ara-74 proAZ ZacYI galK2 rpsL20 xjl-5 mtl-I ] (Boyer & Roulland-Dussoix, 1969) ; MC4100 [F-ara D139 (lad POZYA--argF)U169 rpsL150 relAI fEb-5307 deoCl PtsF25 rbsR] (Casadaban, 1976); LCB128 [as MC4100; torA : : Mud1 (Ap' -lrsc)] (M. Chippaux, Marseilles, France); DSS401 (as MC4100; Adms Km') (Sambasivarao & Weiner, 1991a); and DSS501 (as LCB128; Mms Km") (Sambasivarao & Weiner, 1991a). For overexpression of DmsABC, bacteria were transformed with pDMSl6O (Rothery & Weiner, 1991).…”

Section: Introductionmentioning

confidence: 99%

“…The ability of S-and N-oxides to sustain growth on glycerol minimal media was tested by growing cells in sealed screw-capped tubes containing a small air bubble to allow mixing using a continuously rotating wheel. Quantitative growth experiments were performed in Klett flasks (Sambasivarao & Weiner, 1991a). Assessment of the toxicity of DmsABC substrates by inhibition of anaerobic growth of €.…”

Section: Introductionmentioning

confidence: 99%

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Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase

Simala‐Grant

Weiner

1996

Microbiology

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~~ ~~We have characterized the substrate specificity of dimethyl sulfoxide reductase (DmsABC) of Escherichia coli by determining Km and kut values for 22 different substrates. The enzyme has a very broad substrate specificity. The Km values varied 470-fold, while k,, values varied only 20-fold, implicating K, as the major determinant of kJK, values. Sulfoxides and pyridine N-oxide exhibited the lowest K, values, followed by aliphatic N-oxides. The k,, values for these compounds also followed the same pattern. Substitution at the 2 or 3 position of the pyridine N-oxide ring had little effect on Kw while substitution at the 4 position had a greater effect, and increased Km. Negatively charged substrates were poorly accepted. A few compounds that are not S-or N-oxides were also reduced by the enzyme. Most compounds reduced by DmsABC were not toxic to E. coli under anaerobic growth conditions, and Em coli was able to use many of these compounds anaerobically as terminal electron acceptors in the presence of glycerol. Anaerobic growth on sulfoxides is solely due to DmsABC expression. However, there appears to be another as yet unidentified terminal reductase capable of using pyridine N-oxides as terminal electron acceptors.

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The 1.38 Å crystal structure of DmsD protein from Salmonella typhimurium, a proofreading chaperone on the Tat pathway

et al. 2008

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The DmsD protein is necessary for the biogenesis of dimethyl sulphoxide (DMSO) reductase in many prokaryotes. It performs a critical chaperone function initiated through its binding to the twin-arginine signal peptide of DmsA, the catalytic subunit of DMSO reductase. Upon binding to DmsD, DmsA is translocated to the periplasm via the so-called twin-arginine translocation (Tat) pathway. Here we report the 1.38 A crystal structure of the protein DmsD from Salmonella typhimurium and compare it with a close functional homolog, TorD. DmsD has an all-alpha fold structure with a notable helical extension located at its N-terminus with two solvent exposed hydrophobic residues. A major difference between DmsD and TorD is that TorD structure is a domain-swapped dimer, while DmsD exists as a monomer. Nevertheless, these two proteins have a number of common features suggesting they function by using similar mechanisms. A possible signal peptide-binding site is proposed based on structural similarities. Computational analysis was used to identify a potential GTP binding pocket on similar surfaces of DmsD and TorD structures.

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Differentiation of the multiple S- and N-oxide-reducing activities ofEscherichia coli

Cited by 17 publications

References 24 publications

Investigation of Escherichia coli Dimethyl Sulfoxide Reductase Assembly and Processing in Strains Defective for the sec-Independent Protein Translocation System Membrane Targeting and Translocation

Investigation of Escherichia coli Dimethyl Sulfoxide Reductase Assembly and Processing in Strains Defective for the sec-Independent Protein Translocation System Membrane Targeting and Translocation

Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase

The 1.38 Å crystal structure of DmsD protein from Salmonella typhimurium, a proofreading chaperone on the Tat pathway

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