NarJ subfamily system specific chaperone diversity and evolution is directed by respiratory enzyme associations

Bay, Denice C.; Chan, Catherine B.; Turner, Raymond J.

doi:10.1186/s12862-015-0412-3

Cited by 13 publications

(22 citation statements)

References 70 publications

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“…The NarJ family of REMPs includes DmsD and TorD that chaperone the catalytic subunits during maturation of dimethylsulfoxide and trimethylamine N‐oxide reductases, respectively. Previous bioinformatics analyses of the taxonomically diverse NarJ subfamily revealed a close association between each chaperone and a specific complex iron‐sulfur molybdoenzyme respiratory system, or the operon encoding that system (Bay et al , ). It was also concluded that NarJ members demonstrated the strictest conservation within the subfamily with respect to target sequence motif conservation and their association with operons encoding the respiratory membrane‐bound

{NO}_{3}^{-}

reductase.…”

Section: Discussionmentioning

confidence: 99%

“…Correct folding of complex redox proteins and introduction of cofactors can require chaperones called Redox Enzyme Maturation Proteins (REMPs) (Bay et al , ). NarG is a well‐studied molybdenum (Mo) bis ‐PGD (Mo[PGD] 2 ) binding protein synthesized during anaerobiosis in a range of microorganisms.…”

Section: Introductionmentioning

confidence: 99%

“…In addition, both respiratory and assimilatory

{NO}_{3}^{-}

reductases bind one or more iron‐sulfur cluster(s) to facilitate electron transfer to the active site. For the respiratory

{NO}_{3}^{-}

reductase NarG, it has been previously demonstrated that insertion of the Mo[PGD] 2 cofactor is performed by the chaperone NarJ in E. coli (Blasco et al , ; Blasco et al , ; Bay et al , ). In P. denitrificans , narJ (Pden_4234) also forms an integral part of the narKGHJI gene cluster.…”

Section: Introductionmentioning

confidence: 99%

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A dual functional redox enzyme maturation protein for respiratory and assimilatory nitrate reductases in bacteria

Pinchbeck

Soriano-Laguna

Sullivan

et al. 2019

Molecular Microbiology

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Summary Nitrate is available to microbes in many environments due to sustained use of inorganic fertilizers on agricultural soils and many bacterial and archaeal lineages have the capacity to express respiratory (Nar) and assimilatory (Nas) nitrate reductases to utilize this abundant respiratory substrate and nutrient for growth. Here, we show that in the denitrifying bacterium Paracoccus denitrificans, NarJ serves as a chaperone for both the anaerobic respiratory nitrate reductase (NarG) and the assimilatory nitrate reductase (NasC), the latter of which is active during both aerobic and anaerobic nitrate assimilation. Bioinformatic analysis suggests that the potential for this previously unrecognized role for NarJ in functional maturation of other cytoplasmic molybdenum‐dependent nitrate reductases may be phylogenetically widespread as many bacteria contain both Nar and Nas systems.

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{NO}_{3}^{-}

reductase.…”

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…In addition, both respiratory and assimilatory

{NO}_{3}^{-}

reductases bind one or more iron‐sulfur cluster(s) to facilitate electron transfer to the active site. For the respiratory

{NO}_{3}^{-}

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

A dual functional redox enzyme maturation protein for respiratory and assimilatory nitrate reductases in bacteria

Pinchbeck

Soriano-Laguna

Sullivan

et al. 2019

Molecular Microbiology

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“…Translation at the ribosomes and transport through the membrane can be intimately coupled by action of the signal recognition particle, trigger factor and of the DnaK and GroeEL protein-folding apparatus (Castani e-Cornet, Bruel, & Genevaux, 2014;Saraogi & Shan, 2014). In case of molybdopterin proteins, members of the NarJ family perform a proofreading to check for correct folding before the peptide is directed to the TAT system (Bay, Chan, & Turner, 2015;Chan et al, 2014;Lanciano, Vergnes, Grimaldi, Guigliarelli, & Magalon, 2007). Haems that act in electron transfer, such as c-and b-type haems, or in catalysis by terminal oxidases and nitric oxide reductases (b-, a-and o-type haems) are localised at the outer aspect of the membranes.…”

Section: Assembly Of Bacterial Respiratory Complexesmentioning

confidence: 99%

Bacterial Electron Transfer Chains Primed by Proteomics

Wessels¹,

Almeida²,

Kartal³

et al. 2016

Advances in Bacterial Electron Transport Systems and Their Regulation

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Electron transport phosphorylation is the central mechanism for most prokaryotic species to harvest energy released in the respiration of their substrates as ATP. Microorganisms have evolved incredible variations on this principle, most of these we perhaps do not know, considering that only a fraction of the microbial richness is known. Besides these variations, microbial species may show substantial versatility in using respiratory systems. In connection herewith, regulatory mechanisms control the expression of these respiratory enzyme systems and their assembly at the translational and posttranslational levels, to optimally accommodate changes in the supply of their energy substrates. Here, we present an overview of methods and techniques from the field of proteomics to explore bacterial electron transfer chains and their regulation at levels ranging from the whole organism down to the Ångstrom scales of protein structures. From the survey of the literature on this subject, it is concluded that proteomics, indeed, has substantially contributed to our comprehending of bacterial respiratory mechanisms, often in elegant combinations with genetic and biochemical approaches. However, we also note that advanced proteomics offers a wealth of opportunities, which have not been exploited at all, or at best underexploited in hypothesis-driving and hypothesis-driven research on bacterial bioenergetics. Examples obtained from the related area of mitochondrial oxidative phosphorylation research, where the application of advanced proteomics is more common, may illustrate these opportunities.

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“…The localization of the cofactor within the enzyme suggested that chaperones are required to facilitate the insertion of the complex bis-MGD cofactor into their active sites by the involvement of a final folding step of the target enzyme after bis-MGD insertion [ 6 – 13 ]. For enzymes of the DMSO reductase family, these chaperones are also referred to as redox enzyme maturation proteins (REMPs) [ 14 ]. In general, these chaperones are highly specific for their target enzyme [ 15 ].…”

Section: Introductionmentioning

confidence: 99%

Same but different: Comparison of two system-specific molecular chaperones for the maturation of formate dehydrogenases

et al. 2018

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The maturation of bacterial molybdoenzymes is a complex process leading to the insertion of the bulky bis-molybdopterin guanine dinucleotide (bis-MGD) cofactor into the apo-enzyme. Most molybdoenzymes were shown to contain a specific chaperone for the insertion of the bis-MGD cofactor. Formate dehydrogenases (FDH) together with their molecular chaperone partner seem to display an exception to this specificity rule, since the chaperone FdhD has been proven to be involved in the maturation of all three FDH enzymes present in Escherichia coli. Multiple roles have been suggested for FdhD-like chaperones in the past, including the involvement in a sulfur transfer reaction from the l-cysteine desulfurase IscS to bis-MGD by the action of two cysteine residues present in a conserved CXXC motif of the chaperones. However, in this study we show by phylogenetic analyses that the CXXC motif is not conserved among FdhD-like chaperones. We compared in detail the FdhD-like homologues from Rhodobacter capsulatus and E. coli and show that their roles in the maturation of FDH enzymes from different subgroups can be exchanged. We reveal that bis-MGD-binding is a common characteristic of FdhD-like proteins and that the cofactor is bound with a sulfido-ligand at the molybdenum atom to the chaperone. Generally, we reveal that the cysteine residues in the motif CXXC of the chaperone are not essential for the production of active FDH enzymes.

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NarJ subfamily system specific chaperone diversity and evolution is directed by respiratory enzyme associations

Cited by 13 publications

References 70 publications

A dual functional redox enzyme maturation protein for respiratory and assimilatory nitrate reductases in bacteria

A dual functional redox enzyme maturation protein for respiratory and assimilatory nitrate reductases in bacteria

Bacterial Electron Transfer Chains Primed by Proteomics

Same but different: Comparison of two system-specific molecular chaperones for the maturation of formate dehydrogenases

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