QueE: A Radical SAM Enzyme Involved in the Biosynthesis of 7-Deazapurine Containing Natural Products

Lewis, Julia K.; Bruender, Nathan A.; Bandarian, Vahe

doi:10.1016/bs.mie.2018.05.001

Cited by 7 publications

(5 citation statements)

References 46 publications

(77 reference statements)

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“…QueE has been extensively characterized and contains a single 4Fe-4S cluster, which binds and upon reduction to the +1 state activates the SAM for reductive cleavage to form dAdo⋅. The dAdo⋅ initiates the catalytic cycle by H-atom transfer from the substrate ( 30 , 35 , 48 , 49 , 50 , 51 , 52 ). The reaction catalyzed by QueE is catalytic in SAM, as the cofactor is reformed upon formation of CDG ( 48 ).…”

Section: Resultsmentioning

confidence: 99%

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Intermolecular electron transfer in radical SAM enzymes as a new paradigm for reductive activation

Eastman

Jochimsen

Bandarian

2023

Journal of Biological Chemistry

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Section: Resultsmentioning

confidence: 99%

“…QueE and CPH 4 were expressed and purified as described ( 51 ). Prereduced QueE was generated using the same reconstitution method as described for PapB.…”

Section: Methodsmentioning

confidence: 99%

Intermolecular electron transfer in radical SAM enzymes as a new paradigm for reductive activation

Eastman

Jochimsen

Bandarian

2023

Journal of Biological Chemistry

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“…Specifically, QueE (also called 7-carboxy-7-deazaguanine or CDG synthase) catalyzes the conversion of the substrate CPH 4 (6-carboxy-5,6,7,8-tetrahydropterin) to CDG (7-carboxy-7-deazaguanine) [19,20]. The role of QueE in the biosynthesis of Q has been well characterized, and crystal structures of QueE homologs from Bacillus subtilis, Burkholderia multivorans, and Escherichia coli have been solved, providing insights into the catalytic mechanism [19][20][21][22]. More recently, a second function for QueE has been described during the stress response of E. coli cells exposed to sub-MIC levels of cationic-antimicrobial peptides (AMP) [10].…”

Section: Introductionmentioning

confidence: 99%

Queuosine biosynthetic enzyme, QueE moonlights as a cell division regulator

Adeleye,

Yadavalli

2024

PLoS Genet

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In many organisms, stress responses to adverse environments can trigger secondary functions of certain proteins by altering protein levels, localization, activity, or interaction partners. Escherichia coli cells respond to the presence of specific cationic antimicrobial peptides by strongly activating the PhoQ/PhoP two-component signaling system, which regulates genes important for growth under this stress. As part of this pathway, a biosynthetic enzyme called QueE, which catalyzes a step in the formation of queuosine (Q) tRNA modification is upregulated. When cellular QueE levels are high, it co-localizes with the central cell division protein FtsZ at the septal site, blocking division and resulting in filamentous growth. Here we show that QueE affects cell size in a dose-dependent manner. Using alanine scanning mutagenesis of amino acids in the catalytic active site, we pinpoint residues in QueE that contribute distinctly to each of its functions–Q biosynthesis or regulation of cell division, establishing QueE as a moonlighting protein. We further show that QueE orthologs from enterobacteria like Salmonella typhimurium and Klebsiella pneumoniae also cause filamentation in these organisms, but the more distant counterparts from Pseudomonas aeruginosa and Bacillus subtilis lack this ability. By comparative analysis of E. coli QueE with distant orthologs, we elucidate a unique region in this protein that is responsible for QueE’s secondary function as a cell division regulator. A dual-function protein like QueE is an exception to the conventional model of “one gene, one enzyme, one function”, which has divergent roles across a range of fundamental cellular processes including RNA modification and translation to cell division and stress response.

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“…Specifically, QueE (also called 7-carboxy-7-deazaguanine or CDG synthase) catalyzes the conversion of the substrate CPH4 (6-carboxy-5,6,7,8-tetrahydropterin) to CDG (7-carboxy-7deazaguanine) (23). The role of QueE in the biosynthesis of Q has been well characterized, and crystal structures of QueE homologs from Bacillus subtilis, Burkholderia multivorans, and Escherichia coli have been solved, providing insights into the catalytic mechanism (24)(25)(26)(27). More recently, a second function for QueE has been described during the stress response of E. coli cells exposed to sub-MIC levels of cationic-antimicrobial peptides (AMP) (14).…”

Section: Introductionmentioning

confidence: 99%

Queuosine biosynthetic enzyme, QueE moonlights as a cell division regulator

Adeleye,

Yadavalli

2023

Preprint

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In many organisms, stress responses to adverse environments can trigger secondary functions of certain proteins by altering protein levels, localization, activity, or interaction partners.Escherichia colicells respond to the presence of specific cationic antimicrobial peptides by strongly activating the PhoQ/PhoP two-component signaling system, which regulates genes important for growth under this stress. As part of this pathway, a biosynthetic enzyme called QueE, which catalyzes a step in the formation of queuosine (Q) tRNA modification is upregulated. When cellular QueE levels are high, it co-localizes with the central cell division protein FtsZ at the septal site, blocking division and resulting in filamentous growth. Here we show that QueE affects cell size in a dose-dependent manner. Using alanine scanning mutagenesis of amino acids in the catalytic active site, we pinpoint particular residues in QueE that contribute distinctly to each of its functions – Q biosynthesis or regulation of cell division, establishing QueE as a moonlighting protein. We further show that QueE orthologs from enterobacteria likeSalmonella typhimuriumandKlebsiella pneumoniaealso cause filamentation in these organisms, but the more distant counterparts fromPseudomonas aeruginosaandBacillus subtilislack this ability. By comparative analysis ofE. coliQueE with distant orthologs, we elucidate a unique region in this protein that is responsible for QueE’s secondary function as a cell division regulator. A dual-function protein like QueE is an exception to the conventional model of “one gene, one enzyme, one function”, which has divergent roles across a range of fundamental cellular processes including RNA modification and translation to cell division and stress response.

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QueE: A Radical SAM Enzyme Involved in the Biosynthesis of 7-Deazapurine Containing Natural Products

Cited by 7 publications

References 46 publications

Intermolecular electron transfer in radical SAM enzymes as a new paradigm for reductive activation

Intermolecular electron transfer in radical SAM enzymes as a new paradigm for reductive activation

Queuosine biosynthetic enzyme, QueE moonlights as a cell division regulator

Queuosine biosynthetic enzyme, QueE moonlights as a cell division regulator

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