Peroxide-Shunt Substrate-Specificity for the Salmonella typhimurium O<sub>2</sub>-Dependent tRNA Modifying Monooxygenase (MiaE)

Corder, Andra L.; Subedi, Bishnu P.; Zhang, Siai; Dark, Amanda M.; Foss, Frank W.; Pierce, Brad S.

doi:10.1021/bi4000832

Cited by 17 publications

(35 citation statements)

References 82 publications

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“…It is generally accepted that tRNA 2MeSiPR monooxygenase (MiaE), the only enzyme known to hydroxylate tRNA-bound iP, synthesizes 2MeScZRMP and cZRMP [ 10 , 51 , 61 ]. Yet, trans -selective hydroxylation of tRNA-bound iPR or 2MeSiPR by the same enzyme was reported by others [ 62 , 63 ]. The origin of zeatins in the tRNA of some organisms is entirely unclear, as the presence of the miaE gene is reportedly limited to a few bacterial genera [ 64 ]; however, up-to-date results of BLASTp searches (not shown) using MiaE from Pseudomonas putida [ 65 ] as a query suggests the far wider distribution of MiaE among bacteria than previously anticipated.…”

Section: Formation Of Trans -Zeatin: Unclarified Pathwayssupporting

confidence: 69%

Biochemical and Structural Aspects of Cytokinin Biosynthesis and Degradation in Bacteria

Frébortová

Frébort

2021

Microorganisms

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It has been known for quite some time that cytokinins, hormones typical of plants, are also produced and metabolized in bacteria. Most bacteria can only form the tRNA-bound cytokinins, but there are examples of plant-associated bacteria, both pathogenic and beneficial, that actively synthesize cytokinins to interact with their host. Similar to plants, bacteria produce diverse cytokinin metabolites, employing corresponding metabolic pathways. The identification of genes encoding the enzymes involved in cytokinin biosynthesis and metabolism facilitated their detailed characterization based on both classical enzyme assays and structural approaches. This review summarizes the present knowledge on key enzymes involved in cytokinin biosynthesis, modifications, and degradation in bacteria, and discusses their catalytic properties in relation to the presence of specific amino acid residues and protein structure.

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Section: Formation Of Trans -Zeatin: Unclarified Pathwayssupporting

confidence: 69%

Biochemical and Structural Aspects of Cytokinin Biosynthesis and Degradation in Bacteria

Frébortová

Frébort

2021

Microorganisms

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“…This is twice the expected 24 kDa mass for a single copy of the protein, indicating that Pp-MiaE forms a stable homodimer (α 2 ) in solution (SI, Supplementary Figure S2–2 ). Although this dimeric α 2 configuration of Pp-MiaE is the most commonly observed quaternary structures among the non-heme diiron enzymes family, this result is surprisingly in stark contrast of that reported for the monomeric MiaE from S. typhimurium ( 27 , 28 ). Early bioinformatic sequences analyses of enzymes involved in the biosynthesis pathway of ms 2 io 6 A 37 revealed that MiaE proteins clusters mainly into two groups ( 31 ).…”

Section: Resultscontrasting

confidence: 78%

“…The absorption spectrum of as-isolated Pp-MiaE reveals, in addition to the band at 280 nm corresponding to protein absorption, two distinct bands at 320 and 370 nm (Figure 2A ). This is typical of oxygen-bridged dinuclear non-heme iron systems and are attributable to an oxo-to-Fe III charge transfer transition as observed for MiaE from S. thyhimurium ( 27 , 28 ) and other proteins containing μ-oxo-bridged diiron clusters, including ribonucleotide reductase (RNR) and stearoyl-ACP desaturase (Δ 9 D) ( 42 , 57 ). Similarity to these enzymes is further supported by EPR spectroscopy.…”

Section: Resultsmentioning

confidence: 76%

Structural, biochemical and functional analyses of tRNA-monooxygenase enzyme MiaE from Pseudomonas putida provide insights into tRNA/MiaE interaction

Carpentier

Leprêtre

Basset

et al. 2020

Nucleic Acids Research

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MiaE (2-methylthio-N6-isopentenyl-adenosine37-tRNA monooxygenase) is a unique non-heme diiron enzyme that catalyzes the O2-dependent post-transcriptional allylic hydroxylation of a hypermodified nucleotide 2-methylthio-N6-isopentenyl-adenosine (ms2i6A37) at position 37 of selected tRNA molecules to produce 2-methylthio-N6–4-hydroxyisopentenyl-adenosine (ms2io6A37). Here, we report the in vivo activity, biochemical, spectroscopic characterization and X-ray crystal structure of MiaE from Pseudomonas putida. The investigation demonstrates that the putative pp-2188 gene encodes a MiaE enzyme. The structure shows that Pp-MiaE consists of a catalytic diiron(III) domain with a four alpha-helix bundle fold. A docking model of Pp-MiaE in complex with tRNA, combined with site directed mutagenesis and in vivo activity shed light on the importance of an additional linker region for substrate tRNA recognition. Finally, krypton-pressurized Pp-MiaE experiments, revealed the presence of defined O2 site along a conserved hydrophobic tunnel leading to the diiron active center.

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“…Verification of enzymatic product was performed by multiple reaction monitoring (MRM) using a triple quadrupole LC-MS/MS [Shimadzu Scientific Instruments, LCMS 8040] [34–36]. For each experiment, 10 μL of the benzothiazole standard ( described above ) was injected to determine the product ions and relative distribution for each ion.…”

Section: Methodsmentioning

confidence: 99%

Thiol dioxygenase turnover yields benzothiazole products from 2-mercaptoaniline and O2-dependent oxidation of primary alcohols

Morrow

Sardar

Thapa

et al. 2017

Archives of Biochemistry and Biophysics

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Thiol dioxygenases are non-heme mononuclear iron enzymes that catalyze the O2-dependent oxidation of free thiols (-SH) to produce the corresponding sulfinic acid (-SO2−). Previous chemical rescue studies identified a putative FeIII-O2•− intermediate that precedes substrate oxidation in Mus musculus cysteine dioxygenase (Mm CDO). Given that a similar reactive intermediate has been identified in the extradiol dioxygenase 2, 3-HCPD, it is conceivable that these enzymes share other mechanistic features with regard to substrate oxidation. To explore this possibility, enzymatic reactions with Mm CDO (as well as the bacterial 3-mercaptopropionic acid dioxygenase, Av MDO) were performed using a substrate analogue (2-mercaptoaniline, 2ma). This aromatic thiol closely approximates the catecholic substrate of homoprotocatechuate of 2, 3-HPCD while maintaining the 2-carbon thiol-amine separation preferred by Mm CDO. Remarkably, both enzymes exhibit 2ma-gated O2-consumption; however, none of the expected products for thiol dioxygenase or intra/extradiol dioxygenase reactions were observed. Instead, benzothiazoles are produced by the condensation of 2ma with aldehydes formed by an off-pathway oxidation of primary alcohols added to aqueous reactions to solubilize the substrate. The observed oxidation of 1°-alcohols in 2ma-reactions is consistent with the formation of a high-valent intermediate similar to what has been reported for cytochrome P450 and mononuclear iron model complexes.

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Peroxide-Shunt Substrate-Specificity for the Salmonella typhimurium O₂-Dependent tRNA Modifying Monooxygenase (MiaE)

Cited by 17 publications

References 82 publications

Biochemical and Structural Aspects of Cytokinin Biosynthesis and Degradation in Bacteria

Biochemical and Structural Aspects of Cytokinin Biosynthesis and Degradation in Bacteria

Structural, biochemical and functional analyses of tRNA-monooxygenase enzyme MiaE from Pseudomonas putida provide insights into tRNA/MiaE interaction

Thiol dioxygenase turnover yields benzothiazole products from 2-mercaptoaniline and O2-dependent oxidation of primary alcohols

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Peroxide-Shunt Substrate-Specificity for the Salmonella typhimurium O2-Dependent tRNA Modifying Monooxygenase (MiaE)

Cited by 17 publications

References 82 publications

Biochemical and Structural Aspects of Cytokinin Biosynthesis and Degradation in Bacteria

Biochemical and Structural Aspects of Cytokinin Biosynthesis and Degradation in Bacteria

Structural, biochemical and functional analyses of tRNA-monooxygenase enzyme MiaE from Pseudomonas putida provide insights into tRNA/MiaE interaction

Thiol dioxygenase turnover yields benzothiazole products from 2-mercaptoaniline and O2-dependent oxidation of primary alcohols

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Peroxide-Shunt Substrate-Specificity for the Salmonella typhimurium O₂-Dependent tRNA Modifying Monooxygenase (MiaE)