2.8-Å Cryo-EM Structure of the Large Ribosomal Subunit from the Eukaryotic Parasite Leishmania

Moran Shalev-Benami, Yan Zhang, Donna Matzov, Yehuda Halfon, Arie Zackay, Haim Rozenberg, Ella Zimmerman, Anat Bashan, Charles L. Jaffe, Ada Yonath*, Georgios Skiniotis

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

60 Scopus citations

Abstract

Leishmania is a single-cell eukaryotic parasite of the Trypanosomatidae family, whose members cause an array of tropical diseases. The often fatal outcome of infections, lack of effective vaccines, limited selection of therapeutic drugs, and emerging resistant strains, underline the need to develop strategies to combat these pathogens. The Trypanosomatid ribosome has recently been highlighted as a promising therapeutic target due to structural features that are distinct from other eukaryotes. Here, we present the 2.8-Å resolution structure of the Leishmania donovani large ribosomal subunit (LSU) derived from a cryo-EM map, further enabling the structural observation of eukaryotic rRNA modifications that play a significant role in ribosome assembly and function. The structure illustrates the unique fragmented nature of leishmanial LSU rRNA and highlights the irregular distribution of rRNA modifications in Leishmania, a characteristic with implications for anti-parasitic drug development.

Original languageEnglish
Pages (from-to)288-294
Number of pages7
JournalCell Reports
Volume16
Issue number2
DOIs
StatePublished - 12 Jul 2016

Bibliographical note

Publisher Copyright:
© 2016

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