Yaser Hashem
University of Bordeaux
63 Papers
139 Citations
Yaser Hashem is an academic researcher from University of Bordeaux. The author has contributed to research in topics: Ribosome & Ribosomal RNA. The author has an hindex of 24, co-authored 60 publications. Previous affiliations of Yaser Hashem include Case Western Reserve University & Centre national de la recherche scientifique.
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Papers
Structure of mammalian eIF3 in the context of the 43S preinitiation complex
Amedee des Georges,Vidya Dhote,Lauriane Kuhn,Christopher U.T. Hellen,Tatyana V. Pestova,Joachim Frank,Yaser Hashem +6 more
TL;DR: A cryo-electron microscopy structure of eIF3 is presented in the context of the DHX29-bound 43S complex, showing the PCI/MPN core at ∼6 Å resolution and revealing the organization of the individual subunits and their interactions with components of the 43Scomplex.
Hepatitis-C-virus-like internal ribosome entry sites displace eIF3 to gain access to the 40S subunit.
Yaser Hashem,Amedee des Georges,Amedee des Georges,Vidya Dhote,Robert Langlois,Hstau Y. Liao,Robert A. Grassucci,Tatyana V. Pestova,Christopher U.T. Hellen,Joachim Frank,Joachim Frank +10 more
TL;DR: A role is suggested for the specific interaction of HCV-like IRESs with eIF3 in preventing ribosomal association of eif3, which could serve two purposes: relieving the competition between the IRES and eIF2 for a common binding site on the 40S subunit, and reducing formation of 43S complexes, thereby favouring translation of viral mRNAs.
High-resolution cryo-electron microscopy structure of the Trypanosoma brucei ribosome
Yaser Hashem,Amedee des Georges,Jie Fu,Sarah N. Buss,Fabrice Jossinet,Amy Jobe,Qin Zhang,Hstau Y. Liao,Robert A. Grassucci,Chandrajit L. Bajaj,Eric Westhof,Susan Madison-Antenucci,Joachim Frank,Joachim Frank +13 more
TL;DR: The structure reveals the five cleavage sites of the kinetoplastid large ribosomal subunit (LSU) rRNA chain, and suggests that the cleavage is important for the maintenance of the T. brucei ribosome in the observed structure, and discusses several possible implications of the large rRNA expansion segments for the translation-regulation process.
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The ABC-F protein EttA gates ribosome entry into the translation elongation cycle.
Grégory Boël,Paul Smith,Wei Ning,Michael T. Englander,Bo Chen,Yaser Hashem,Anthony J Testa,Jeffrey J. Fischer,Hans-Joachim Wieden,Joachim Frank,Ruben L. Gonzalez,John F. Hunt,John F. Hunt +12 more
TL;DR: It is demonstrated that YjjK, the most prevalent eubacterial ABC-F protein, gates ribosome entry into the translation elongation cycle through a nucleotide-dependent interaction sensitive to ATP/ADP ratio.
Embraced by eIF3: structural and functional insights into the roles of eIF3 across the translation cycle.
Leoš Shivaya Valášek,Jakub Zeman,Susan Wagner,Petra Beznosková,Zuzana Pavlíková,Mahabub Pasha Mohammad,Vladislava Hronová,Anna Herrmannová,Yaser Hashem,Stanislava Gunišová +9 more
TL;DR: Recent structural views of the eIF3–40S complex are united and all known eif3 roles are discus to provide a broad picture of theeIF3’s impact on translational control in eukaryotic cells.
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