Premium
Altered binding of eukaryotic Elongation Factor 3 (eEF3) to the ribosomes: A key to understanding its functional requirement in yeast
Author(s) -
Sasikumar Arjun Narayan,
Kinzy Terri Goss
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.467.8
Subject(s) - elongation factor , ribosome , translation (biology) , microbiology and biotechnology , biology , eukaryotic ribosome , initiation factor , saccharomyces cerevisiae , protein biosynthesis , eif4e , yeast , biochemistry , messenger rna , rna , gene
Translational elongation is a universally conserved process. In eukaryotes this involves two G‐proteins: eukaryotic Elongation Factor 1A (eEF1A), required for loading the cognate aminoacyl‐tRNA at the A‐site of the ribosome and eukaryotic Elongation Factor 2 (eEF2), essential for the translocation of the ribosome along the mRNA. Fungal translation is unique in its requirement for the ATPase eEF3. An essential protein with no known mammalian homologue, eEF3 is an ideal anti‐fungal drug target. eEF3‐ribosome binding is modulated by Stm1p, a non‐essential protein implicated in translation under nutrient stress. Our work shows that knocking out Stm1p adversely affects the ability of Cryptococcus neoformans eEF3 to complement the loss of WT eEF3 in Saccharomyces cerevisiae , reinforcing the functional relationship between the two. We also show that mutations in the chromodomain of eEF3 affect ribosome binding and cause semi‐dominant slow growth phenotypes. Studying the effects of altered ribosome binding of eEF3 will provide insights in its role in fungal translation. This work is supported by the National Institutes of Health.