Structures of KEOPS bound to tRNA reveal functional roles of the kinase Bud32.

ABSTRACT: The enzyme complex KEOPS (Kinase, Endopeptidase and Other Proteins of Small size) installs the universally conserved and essential N⁶-threonylcarbamoyl adenosine modification (t⁶A) on ANN-decoding tRNAs in eukaryotes and in archaea. KEOPS consists of Cgi121, Kae1, Pcc1, Gon7 and the atypical kinase/ATPase Bud32. Except Gon7, all KEOPS subunits are needed for tRNA modification, and in humans, mutations in all five genes underlie the lethal genetic disease Galloway Mowat Syndrome (GAMOS). Kae1 catalyzes the modification of tRNA, but the specific contributions of Bud32 and the other subunits are less clear. Here we solved cryogenic electron microscopy structures of KEOPS with and without a tRNA substrate. We uncover distinct flexibility of KEOPS-bound tRNA revealing a co

SUBMITTER: Ona Chuquimarca SM 

PROVIDER: S-EPMC11621456 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature