The regulation of Moco biosynthesis and molybdoenzyme gene expression by molybdenum and iron in bacteria

Zupok, Arkadiusz; Iobbi‐Nivol, Chantal; Méjean, Vincent; Leimkühler, Silke

doi:10.1039/c9mt00186g

Cited by 19 publications

(30 citation statements)

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“…According to previous studies, MoaD-MoaE in molybdenum cofactor (Moco) biosynthesis was able to catalyze some redox reactions in vivo (Zupok et al, 2019). In the present study, we found the expression levels of DRMoaE and DRJAMM are increased simultaneously under oxidative stress, indicating that DRJAMM is necessary for DRMoaE activation.…”

Section: Discussionsupporting

confidence: 69%

“…Recently, dr_0402 has been found to encode the JAMM/MPN protein, and the product of its expression, DRJAMM, could cleave the MoaD-MoaE fusion protein (DR2607) and generate a C-terminal Gly residue (Yang et al, 2018). MoaD-MoaE is known as the MPT synthase that catalyzes the formation of MPT from cyclic pyranopterin monophosphate (cPMP) converted from 5 -GTP, while the two sulfur molecules on cPMP are carried as thiosulfates on the C-terminal glycine of MoaD (Leimkuhler et al, 2001;Zupok et al, 2019). During the formation of MPT, the substrate pocket of MoaE can bound the cPMP, MPT, and the C-terminal of MoaD.…”

Section: Introductionmentioning

confidence: 99%

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DRJAMM Is Involved in the Oxidative Resistance in Deinococcus radiodurans

et al. 2022

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Proteins containing JAB1/MPN/MOV34 metalloenzyme (JAMM/MPN+) domains that have Zn2+-dependent deubiquitinase (DUB) activity are ubiquitous across among all domains of life. Recently, a homolog in Deinococcus radiodurans, DRJAMM, was reported to possess the ability to cleave DRMoaD-MoaE. However, the detailed biochemical characteristics of DRJAMM in vitro and its biological mechanism in vivo remain unclear. Here, we show that DRJAMM has an efficient in vitro catalytic activity in the presence of Mn2+, Ca2+, Mg2+, and Ni2+ in addition to the well-reported Zn2+, and strong adaptability at a wide range of temperatures. Disruption of drJAMM led to elevated sensitivity in response to H2O2in vivo compared to the wild-type R1. In particular, the expression level of MoaE, a product of DRJAMM cleavage, was also increased under H2O2 stress, indicating that DRJAMM is needed in the antioxidant process. Moreover, DRJAMM was also demonstrated to be necessary for dimethyl sulfoxide respiratory system in D. radiodurans. These data suggest that DRJAMM plays key roles in the process of oxidative resistance in D. radiodurans with multiple-choice of metal ions and temperatures.

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Section: Discussionsupporting

confidence: 69%

Section: Introductionmentioning

confidence: 99%

DRJAMM Is Involved in the Oxidative Resistance in Deinococcus radiodurans

et al. 2022

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“…Two binding sites of CsrA were identified within the moaA promoter region (Patterson-Fortin et al, 2013). For Moco biosynthesis, CsrA was shown to activate the transcription, and it has been suggested that CsrA enhances Moco biosynthesis under conditions of high demand (Zupok et al, 2019b).…”

Section: The Regulation Of Moco Biosynthesismentioning

confidence: 99%

The biosynthesis of the molybdenum cofactors in Escherichia coli

Leimkühler

2020

Environmental Microbiology

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The biosynthesis of the molybdenum cofactor (Moco) is highly conserved among all kingdoms of life. In all molybdoenzymes containing Moco, the molybdenum atom is coordinated to a dithiolene group present in the pterin-based 6-alkyl side chain of molybdopterin (MPT). In general, the biosynthesis of Moco can be divided into four steps in in bacteria: (i) the starting point is the formation of the cyclic pyranopterin monophosphate (cPMP) from 5 0 -GTP, (ii) in the second step the two sulfur atoms are inserted into cPMP leading to the formation of MPT, (iii) in the third step the molybdenum atom is inserted into MPT to form Moco and (iv) in the fourth step bis-Mo-MPT is formed and an additional modification of Moco is possible with the attachment of a nucleotide (CMP or GMP) to the phosphate group of MPT, forming the dinucleotide variants of Moco. This review presents an update on the well-characterized Moco biosynthesis in the model organism Escherichia coli including novel discoveries from the recent years.

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“…In addition, the l-cysteine desulfurase IscS is shared between Fe-S cluster assembly and Moco biosynthesis since it also mobilizes the sulfur for the synthesis of the dithiolene group present in Moco. Further, the expression of most molybdoenzymes and proteins involved in Moco biosynthesis in bacteria is regulated by the transcriptional regulator for fumarate and nitrate reduction, FNR [78,79]. The activity of FNR itself is directly dependent on the availability of Fe-S clusters under anaerobic conditions; consequently, Moco is not synthesized and molybdoenzymes are not expressed when Fe-S clusters are not assembled (Figure 4).…”

Section: Linking Moco Biosynthesis and Fe-s Cluster Assembly In Bacteriamentioning

confidence: 99%

The Requirement of Inorganic Fe-S Clusters for the Biosynthesis of the Organometallic Molybdenum Cofactor

et al. 2020

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Iron-sulfur (Fe-S) clusters are essential protein cofactors. In enzymes, they are present either in the rhombic [2Fe-2S] or the cubic [4Fe-4S] form, where they are involved in catalysis and electron transfer and in the biosynthesis of metal-containing prosthetic groups like the molybdenum cofactor (Moco). Here, we give an overview of the assembly of Fe-S clusters in bacteria and humans and present their connection to the Moco biosynthesis pathway. In all organisms, Fe-S cluster assembly starts with the abstraction of sulfur from l-cysteine and its transfer to a scaffold protein. After formation, Fe-S clusters are transferred to carrier proteins that insert them into recipient apo-proteins. In eukaryotes like humans and plants, Fe-S cluster assembly takes place both in mitochondria and in the cytosol. Both Moco biosynthesis and Fe-S cluster assembly are highly conserved among all kingdoms of life. Moco is a tricyclic pterin compound with molybdenum coordinated through its unique dithiolene group. Moco biosynthesis begins in the mitochondria in a Fe-S cluster dependent step involving radical/S-adenosylmethionine (SAM) chemistry. An intermediate is transferred to the cytosol where the dithiolene group is formed, to which molybdenum is finally added. Further connections between Fe-S cluster assembly and Moco biosynthesis are discussed in detail.

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The regulation of Moco biosynthesis and molybdoenzyme gene expression by molybdenum and iron in bacteria

Abstract: The regulation of the operons involved in Moco biosynthesis is dependent on the availability of Fe–S clusters in the cell.

Cited by 19 publications

References 257 publications

DRJAMM Is Involved in the Oxidative Resistance in Deinococcus radiodurans

DRJAMM Is Involved in the Oxidative Resistance in Deinococcus radiodurans

The biosynthesis of the molybdenum cofactors in Escherichia coli

The Requirement of Inorganic Fe-S Clusters for the Biosynthesis of the Organometallic Molybdenum Cofactor

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