Identification and characterization of the missing phosphatase on the riboflavin biosynthesis pathway in <i>Arabidopsis thaliana</i>

Sa, Na; Rawat, Renu; Thornburg, Chelsea K.; Walker, Kevin D.; Roje, Sanja

doi:10.1111/tpj.13291

Cited by 37 publications

(40 citation statements)

References 47 publications

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“…Taken together, these experiments definitively pinpointed the bacterial metabolite necessary to generate activating MAIT cell ligands as 5‐A‐RU. These studies have now been recapitulated for E. coli and S. pneumoniae by other groups, and also demonstrate the requirement for ribD/G in these bacteria …”

Section: Discovery Of Mr1 Bound Antigens That Activate Mait Cellssupporting

confidence: 56%

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An overview on the identification of MAIT cell antigens

et al. 2018

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Mucosal associated invariant T (MAIT) cells are restricted by the monomorphic MHC class I-like molecule, MHC-related protein-1 (MR1). Until 2012, the origin of the MAIT cell antigens (Ags) was unknown, although it was established that MAIT cells could be activated by a broad range of bacteria and yeasts, possibly suggesting a conserved Ag. Using a combination of protein chemistry, mass spectrometry, cellular biology, structural biology and small molecule chemistry, we discovered MR1 ligands derived from folic acid (vitamin B9) and from an intermediate in the microbial biosynthesis of riboflavin (vitamin B2). While the folate derivative 6-formylpterin generally inhibited MAIT cell activation, two riboflavin pathway derivatives, 5-(2-oxopropylideneamino)-6-D-ribitylaminouracil and 5-(2-oxoethylideneamino)-6-D-ribitylaminouracil, were potent MAIT cell agonists. Other intermediates and derivatives of riboflavin synthesis displayed weak or no MAIT cell activation. Collectively, these studies revealed that in addition to peptide and lipid-based Ags, small molecule natural product metabolites are also ligands that can activate T cells expressing αβ T-cell receptors, and here we recount this discovery.

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Section: Discovery Of Mr1 Bound Antigens That Activate Mait Cellssupporting

confidence: 56%

“…A further complication is that the enzyme nomenclature also differs among bacteria. The details of riboflavin synthesis and its regulation are complex and still emerging, with the recent discovery of the 5‐A‐RU 5′‐phosphate phosphatase in Arabidopsis thaliana, completing the pathway.…”

Section: Discovery Of Mr1 Bound Antigens That Activate Mait Cellsmentioning

confidence: 99%

An overview on the identification of MAIT cell antigens

et al. 2018

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“…(Haase et al, 2013;Sarge et al, 2015). The protein AtPyrP2 from Arabidopsis thaliana was found to be very specific for ARPP and silencing of the AtPyrP2 gene led to decreased levels of riboflavin, RP and FAD (Sa et al, 2016). This finding suggests that in plants a riboflavin pathway-specific ARPP phosphatase is present.…”

Section: Ta B L E 1 Substrate Profiles Of Recombinant Roscmentioning

confidence: 96%

The novel phosphatase RosC catalyzes the last unknown step of roseoflavin biosynthesis in Streptomyces davaonensis

Schneider

Konjik

Kißling

et al. 2020

Molecular Microbiology

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is a red riboflavin analog with broad antimicrobial activity against Gram-positive bacteria (Otani et al., 1974). Under laboratory conditions RoF is produced in the stationary phase of growth by two different Gram-positive bacterial species, S. davaonensis (formerly S. davawensis (Landwehr et al., 2018)) and Streptomyces cinnabarinus (Jankowitsch et al., 2012). Other RoF producers are not known. RoF is taken up by target cells by riboflavin importers. Thus, RoF only acts against bacteria having riboflavin importers, which appear to be present mostly in Gram-positive bacteria (Grill

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“…A study from 2011 showed that an FMN-specific hydrolase (AtcpFHy1) from the HAD superfamily was able to catalyze the dephosphorylation of FMN [46]. A few years later, in 2016, the plastidic FMN hydrolase AtcpFHy1 (At1g79790) together with the gene products of At4g11570 and At4g25840, were identified as having ArPP phosphatase activity [47]. In 2015, the HAD superfamily phosphatase EFI-501083 from Bacteroides thetaiotaomicron (B. thetaiotaomicron) was predicted to catalyze the dephosphorylation of ArPP according to covalent docking models [48].…”

Section: Key Enzymes For the Synthesis Of Rfmentioning

confidence: 99%

Production of riboflavin and related cofactors by biotechnological processes

Liu

Wang

et al. 2020

Microb Cell Fact

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Riboflavin (RF) and its active forms, the cofactors flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), have been extensively used in the food, feed and pharmaceutical industries. Modern commercial production of riboflavin is based on microbial fermentation, but the established genetically engineered production strains are facing new challenges due to safety concerns in the food and feed additives industry. High yields of flavin mononucleotide and flavin adenine dinucleotide have been obtained using whole-cell biocatalysis processes. However, the necessity of adding expensive precursors results in high production costs. Consequently, developing microbial cell factories that are capable of efficiently producing flavin nucleotides at low cost is an increasingly attractive approach. The biotechnological processes for the production of RF and its cognate cofactors are reviewed in this article.

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Identification and characterization of the missing phosphatase on the riboflavin biosynthesis pathway in Arabidopsis thaliana

Cited by 37 publications

References 47 publications

An overview on the identification of MAIT cell antigens

An overview on the identification of MAIT cell antigens

The novel phosphatase RosC catalyzes the last unknown step of roseoflavin biosynthesis in Streptomyces davaonensis

Production of riboflavin and related cofactors by biotechnological processes

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