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

Publication date: Available online 30 June 2016
Source:Cell Reports
Author(s): Moran Shalev-Benami, Yan Zhang, Donna Matzov, Yehuda Halfon, Arie Zackay, Haim Rozenberg, Ella Zimmerman, Anat Bashan, Charles L. Jaffe, Ada Yonath, Georgios Skiniotis
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.

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Shalev-Benami et al. describe the structure of the Leishmania donovani large ribosomal subunit (LSU), obtained by cryo-EM at 2.8-Å resolution. The structure shows the fragmented nature of leishmanial rRNA and highlights the irregular distribution of rRNA modifications with implications for drug development against this protozoan parasite, which afflicts millions of people worldwide.


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