Structures and stabilization of kinetoplastid-specific split rRNAs revealed by comparing leishmanial and human ribosomes

Xing Zhang, Mason Lai, Winston Chang, Iris Yu, Ke Ding, Jan Mrazek, Hwee L. Ng, Otto O. Yang, Dmitri A. Maslov and Z. Hong Zhou ()
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Xing Zhang: Center of Cryo Electron Microscopy, Zhejiang University School of Medicine
Mason Lai: Immunology and Molecular Genetics, University of California
Winston Chang: Immunology and Molecular Genetics, University of California
Iris Yu: Immunology and Molecular Genetics, University of California
Ke Ding: Immunology and Molecular Genetics, University of California
Jan Mrazek: David Geffen School of Medicine, University of California Los Angeles
Hwee L. Ng: David Geffen School of Medicine, University of California Los Angeles
Otto O. Yang: California NanoSystems Institute, University of California
Dmitri A. Maslov: University of California
Z. Hong Zhou: California NanoSystems Institute, University of California

Nature Communications, 2016, vol. 7, issue 1, 1-10

Abstract: Abstract The recent success in ribosome structure determination by cryoEM has opened the door to defining structural differences between ribosomes of pathogenic organisms and humans and to understand ribosome-targeting antibiotics. Here, by direct electron-counting cryoEM, we have determined the structures of the Leishmania donovani and human ribosomes at 2.9 Å and 3.6 Å, respectively. Our structure of the leishmanial ribosome elucidates the organization of the six fragments of its large subunit rRNA (as opposed to a single 28S rRNA in most eukaryotes, including humans) and reveals atomic details of a unique 20 amino acid extension of the uL13 protein that pins down the ends of three of the rRNA fragments. The structure also fashions many large rRNA expansion segments. Direct comparison of our human and leishmanial ribosome structures at the decoding A-site sheds light on how the bacterial ribosome-targeting drug paromomycin selectively inhibits the eukaryotic L. donovani, but not human, ribosome.

Date: 2016
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DOI: 10.1038/ncomms13223

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