Stephanie J. Maiocco

Coupling dead cell recognition to Fcγ receptors augments anticancer immunity

Tomas Castro‐Dopico, Cécile Piot, Michael D. Buck, Lucía Gandullo‐Sánchez et autres

Abstract Type 1 conventional dendritic cells (cDC1s) are key antigen-presenting cells (APCs) for cross-priming of CD8 + T cells against cancer. They can capture and cross-present dead cell antigens via DNGR-1 (CLEC9A), a receptor for F-actin exposed on cell corpses. However, cDC1s …

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Cross-presentation of dead cell-associated antigens shapes the neoantigenic landscape of tumor immunity

Kok Haw Jonathan Lim, Oliver Schulz, Irene Lobón, Tomas Castro‐Dopico et autres

Type 1 conventional dendritic cells (cDC1s) acquire and cross-present tumor antigens to prime CD8⁺ T cells. Whether this selects for specific neoantigens is unclear. DNGR-1 (CLEC9A), a cDC1 receptor for F-actin exposed on dead cells, promotes cross-presentation of cell-associated antigens. Here we …

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Escherichia coli Triheme Enzyme YhjA: Structure and Reactivity

Patrick Hewitt, Julian Seidel, Anja Wüst, Stephanie J. Maiocco et autres

It has been recently realized that some Gram-negative organisms such as Escherichia coli produce a multiheme cytochrome c to serve as a quinol peroxidase that couples electrons from the quinol pool directly to H 2 O 2 . The E. coli version …

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Parsing redox potentials of five ferredoxins found within Thermotoga maritima

Stephanie J. Maiocco, Arthur Arcinas, Squire J. Booker, Sean J. Elliott

Abstract Most organisms contain multiple soluble protein‐based redox carriers such as members of the ferredoxin (Fd) family, that contain one or more iron–sulfur clusters. The potential redundancy of Fd proteins is poorly understood, particularly in connection to the ability of Fd proteins …

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Ferredoxins as interchangeable redox components in support of MiaB, a radical S‐adenosylmethionine methylthiotransferase

Arthur Arcinas, Stephanie J. Maiocco, Sean J. Elliott, Alexey V. Silakov et autres

Abstract MiaB is a member of the methylthiotransferase subclass of the radical S‐adenosylmethionine (SAM) superfamily of enzymes, catalyzing the methylthiolation of C2 of adenosines bearing an N6‐isopentenyl (i6A) group found at position 37 in several tRNAs to afford 2‐methylthio‐N6‐(isopentenyl)adenosine (ms2i6A). MiaB uses …

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Determining Redox Potentials of the Iron–Sulfur Clusters of the AdoMet Radical Enzyme Superfamily

Stephanie J. Maiocco, Lindsey M. Walker, Sean J. Elliott

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Molecular basis of cobalamin-dependent RNA modification

Daniel Dowling, Zachary D. Miles, Caroline Köhrer, Stephanie J. Maiocco et autres

Queuosine (Q) was discovered in the wobble position of a transfer RNA (tRNA) 47 years ago, yet the final biosynthetic enzyme responsible for Q-maturation, epoxyqueuosine (oQ) reductase (QueG), was only recently identified. QueG is a cobalamin (Cbl)-dependent, [4Fe-4S] cluster-containing protein that produces …

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Structure of epoxyqueuosine reductase from Bacillus subtilis with the Asp134 catalytic loop swung out of the active site.

Daniel Dowling, Zachary D. Miles, Caroline Köhrer, Stephanie J. Maiocco et autres

Transformations of the FeS Clusters of the Methylthiotransferases MiaB and RimO, Detected by Direct Electrochemistry

Stephanie J. Maiocco, Arthur Arcinas, Bradley J. Landgraf, Kyung-Hoon Lee et autres

) moiety on unactivated carbon centers. These enzymes contain two [4Fe-4S] clusters, one of which participates in the reductive fragmentation of AdoMet to generate a 5'-deoxyadenosyl 5'-radical and the other of which, termed the auxiliary cluster, is believed to play a central …

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Spectroscopic and Electrochemical Characterization of a Unique Radical S‐Adenosylmethionine Methylase

Anthony J. Blaszczyk, Alexey V. Silakov, Bo Zhang, Stephanie J. Maiocco et autres

TsrM catalyzes the methylation of carbon 2 of the indole ring of L‐tryptophan. Its reaction is the first step in the biosynthesis of the unique quinaldic acid moiety of thiostrepton A, a thiopeptide antibiotic. The appended methyl group derives from S‐adenosylmethionine (SAM); …

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Spectroscopic and Electrochemical Characterization of the Iron–Sulfur and Cobalamin Cofactors of TsrM, an Unusual Radical S-Adenosylmethionine Methylase

Anthony J. Blaszczyk, Alexey V. Silakov, Bo Zhang, Stephanie J. Maiocco et autres

TsrM, an annotated radical S-adenosylmethionine (SAM) enzyme, catalyzes the methylation of carbon 2 of the indole ring of L-tryptophan. Its reaction is the first step in the biosynthesis of the unique quinaldic acid moiety of thiostrepton A, a thiopeptide antibiotic. The appended …

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Biophysical characterization of electron transfer proteins containing multiple metallocofactors: investigation of the AdoMet radical and cytochrome c peroxidase enzyme superfamilies

Stephanie J. Maiocco

Metallocofactors are ubiquitous in nature, serving multiple purposes in proteins. These metallocofactors typically act as the site of catalysis or as an electron relay to move electrons within the protein, or within the cell, and are very energetically costly to manufacture. Yet, …