Physical nature of signal peptide binding to DmsD

Winstone, Tara L.; Workentine, Matthew L.; Sarfo, Kwabena J.; Binding, Andrew J.; Haslam, Bronwyn; Turner, Raymond J.

doi:10.1016/j.abb.2006.08.009

Cited by 33 publications

(53 citation statements)

References 24 publications

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“…Here we addressed the question of the structure adopted by the N-terminus of NarG during the recognition process. At first, we synthesized two peptides [NarG (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15) and NarG(1-28)] and solved their structures by NMR; NarG (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15) corresponding to the predicted N-terminal helix and NarG(1-28), which included both the N-terminal helix and the b-sheet present in the mature NarGHI complex. The 1 H, 15 N-heteronuclear single quantum coherence (HSQC) spectra at pH 4.5 of both peptides and medium range NOEs were in agreement with the presence of an a-helix (residues Ser2-Phe11) in both peptides (Figs 1 and 2).…”

Section: Resultsmentioning

confidence: 99%

Basis of recognition between the NarJ chaperone and the N‐terminus of the NarG subunit from Escherichia coli nitrate reductase

et al. 2010

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A novel class of molecular chaperones co‐ordinates the assembly and targeting of complex metalloproteins by binding to an amino‐terminal peptide of the cognate substrate. We have previously shown that the NarJ chaperone interacts with the N‐terminus of the NarG subunit coming from the nitrate reductase complex, NarGHI. In the present study, NMR structural analysis revealed that the NarG(1–15) peptide adopts an α‐helical conformation in solution. Moreover, NarJ recognizes and binds the helical NarG(1–15) peptide mostly via hydrophobic interactions as deduced from isothermal titration calorimetry analysis. NMR and differential scanning calorimetry analysis revealed a modification of NarJ conformation during complex formation with the NarG(1–15) peptide. Isothermal titration calorimetry and BIAcore experiments support a model whereby the protonated state of the chaperone controls the time dependence of peptide interaction. Structured digital abstract • http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-7557484: NarJT (uniprotkb:http://www.ebi.uniprot.org/entry/P0AF26) and NarG (uniprotkb:http://www.ebi.uniprot.org/entry/P09152) bind (http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0407) by isothermal titration calorimetry (http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0065) • http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-7557456: NarJT (uniprotkb:http://www.ebi.uniprot.org/entry/P0AF26) and NarG (uniprotkb:http://www.ebi.uniprot.org/entry/P09152) bind (http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0407) by nuclear magnetic resonance (http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0077)

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Section: Resultsmentioning

confidence: 99%

Basis of recognition between the NarJ chaperone and the N‐terminus of the NarG subunit from Escherichia coli nitrate reductase

et al. 2010

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“…Twinarginine leader peptide binding is a canonical feature of REMPs, and as such, binding of DmsD to the DmsA RRleader peptide is an absolute prerequisite for DMSO reductase biogenesis (26,27). It is clear that DmsD binds the DmsA RR-leader at 1:1 stoichiometry and that the entire hydrophobic region is required for binding (46) although specificity is more difficult to define (47). Phylogenetic analyses found DmsD to be related to system-specific chaperones of other MobisPGD-containing oxidoreductases that included TorD for TMAO reductase and NarJ for cytoplasmic nitrate reductase A, both of which are CISM enzymes related to DMSO reductase (19,25).…”

Section: So Dmso] (4)mentioning

confidence: 99%

Assembly pathway of a bacterial complex iron sulfur molybdoenzyme

Cherak

Turner

2017

Biomolecular Concepts

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Protein folding and assembly into macromolecule complexes within the living cell are complex processes requiring intimate coordination. The biogenesis of complex iron sulfur molybdoenzymes (CISM) requires use of a system specific chaperone -a redox enzyme maturation protein (REMP) -to help mediate final folding and assembly. The CISM dimethyl sulfoxide (DMSO) reductase is a bacterial oxidoreductase that utilizes DMSO as a final electron acceptor for anaerobic respiration. The REMP DmsD strongly interacts with DMSO reductase to facilitate folding, cofactor-insertion, subunit assembly and targeting of the multi-subunit enzyme prior to membrane translocation and final assembly and maturation into a bioenergetic catalytic unit. In this article, we discuss the biogenesis of DMSO reductase as an example of the participant network for bacterial CISM maturation pathways.

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“…The EcDmsD protein was expressed using the plasmid pTDMS67 generated previously by Winstone et al 7 in the host strain C41(DE3). 21 Overnight cultures were diluted (1%) into LB broth containing ampicillin (50 μg/mL), grown at 37 °C for 3 h, and induced with a final concentration of 1 mM IPTG for a further 3 h. Cells were harvested by centrifugation and lysed with an Avestin Emulsiflex-3C cell homogenizer.…”

Section: Expression and Purification Of Ecdmsdmentioning

confidence: 99%

“…6 The REMPs and their corresponding Tat leader peptides appear to form tight associations. 7,8 A number of structures for the REMP proteins are available in the Protein Data Bank (PDB). These include Shewanella massilia TorD (SmTorD; PDB ID 1N1C), 9 Salmonella typhimurium DmsD (StDmsD; PDB ID 1S9U), 10 Archaeoglobus fulgidus AF0173 (PDB ID 2O9X), 11 A. fulgidus AF0160 (PDB ID 2IDG), and, finally, the NMR structure of the E. coli NapD protein (PDB ID 2JSX).…”

Section: Introductionmentioning

confidence: 99%

Structural Analysis of a Monomeric Form of the Twin-Arginine Leader Peptide Binding Chaperone Escherichia coli DmsD

Stevens

Winstone

Turner

et al. 2009

Journal of Molecular Biology

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The redox enzyme maturation proteins play an essential role in the proofreading and membrane targeting of protein substrates to the twin-arginine translocase. Functionally, the most thoroughly characterized redox enzyme maturation protein to date is Escherichia coli DmsD (EcDmsD).Herein, we present the X-ray crystal structure of the monomeric form of the EcDmsD refined to 2.0 Å resolution, with clear electron density present for each of its 204 amino acid residues. The structural data presented here complement the biochemical data previously generated regarding the function of these twin-arginine translocase leader peptide binding chaperone proteins. Docking and molecular dynamics simulation experiments were used to provide a proposed model for how this chaperone is able to recognize the leader peptide of its substrate DmsA. The interactions observed in the model are in agreement with previous biochemical data and suggest intimate interactions between the conserved twin-arginine motif of the leader peptide of E. coli DmsA and the most conserved regions on the surface of EcDmsD.

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Physical nature of signal peptide binding to DmsD

Cited by 33 publications

References 24 publications

Basis of recognition between the NarJ chaperone and the N‐terminus of the NarG subunit from Escherichia coli nitrate reductase

Basis of recognition between the NarJ chaperone and the N‐terminus of the NarG subunit from Escherichia coli nitrate reductase

Assembly pathway of a bacterial complex iron sulfur molybdoenzyme

Structural Analysis of a Monomeric Form of the Twin-Arginine Leader Peptide Binding Chaperone Escherichia coli DmsD

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