Publications by authors named "B Collinet"
In Archaea and Eukaryotes, the synthesis of a universal tRNA modification, N-threonyl-carbamoyl adenosine (tA), is catalyzed by the KEOPS complex composed of Kae1, Bud32, Cgi121, and Pcc1. A fifth subunit, Gon7, is found only in Fungi and Metazoa. Here, we identify and characterize a fifth KEOPS subunit in Archaea.
View Article and Find Full Text PDFThe tRNA modification N6-threonylcarbamoyladenosine (t6A) is universally conserved in all organisms. In bacteria, the biosynthesis of t6A requires four proteins (TsaBCDE) that catalyze the formation of t6A via the unstable intermediate l-threonylcarbamoyl-adenylate (TC-AMP). While the formation and stability of this intermediate has been studied in detail, the mechanism of its transfer to A37 in tRNA is poorly understood.
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- N-threonyl-carbamoylation of adenosine 37 in ANN-type tRNAs is crucial for accurate protein translation, utilizing the YRDC and OSGEP enzymes.
- Mutations in the KEOPS complex subunits have been linked to Galloway-Mowat syndrome, with YRDC mutations causing severe symptoms and GON7 mutations resulting in milder forms.
- The crystal structure of a GON7 subcomplex reveals that GON7 becomes partially structured when interacting with LAGE3, indicating its role in stabilizing the KEOPS complex.
The universal N6-threonylcarbamoyladenosine (t6A) modification at position A37 of ANN-decoding tRNAs is essential for translational fidelity. In bacteria the TsaC enzyme first synthesizes an l-threonylcarbamoyladenylate (TC-AMP) intermediate. In cooperation with TsaB and TsaE, TsaD then transfers the l-threonylcarbamoyl-moiety from TC-AMP onto tRNA.
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