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Mechanism and regulation of translation elongation
Author(s) -
Kinzy Terri Goss,
Esposito Anthony,
He Dongming,
Hutton Jenna,
Lewis Marcus,
Mateyak Maria,
Ranaweera Siripala,
Sasikumar Arjun
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.79.3
Subject(s) - elongation factor , translation (biology) , eukaryotic translation , diphtheria toxin , ribosome , protein biosynthesis , biology , microbiology and biotechnology , saccharomyces cerevisiae , elongation , biochemistry , yeast , rna , gene , toxin , messenger rna , materials science , ultimate tensile strength , metallurgy
The mechanism of elongation during protein synthesis has many similarities between bacteria and eukaryotes. However, many unique aspects of elongation are found in eukaryotic systems, including some that can be capitalized on to treat infectious diseases. The eukaryotic elongation factor 1A (eEF1A) binds and bundles actin, which when altered affects gene expression at the level of initiation of translation. eEF2 is subject to ADP ribosylation by bacterial toxins from Corynebacterium diphtheria and Pseudomonas aeruginosa . This leads to inhibition of its function in translation elongation. A novel Saccharomyces cerevisiae system has been established to directly address the effects of ADP‐ribosylation on eEF2's role in translation elongation in vivo. This system employs eEF2 mutations identified within the anticodon mimicry domain which display dominant resistance to galactose‐induced diphtheria toxin and also help demonstrate the key interactions required for translocation. eEF3 is a fungal specific proteins required for elongation in vitro and in vivo. The interaction of this protein with the ribosome appears to be linked to the activity of Stm1p. The nature of this interaction, and the role of a chromodomain like insertion in the second ATP binding domain of eEF3, likely play key roles in the mechanism of action of this protein.