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CAP INDEPENDENT TRANSLATION CONTROLS IN BARLEY YELLOW DWARF VIRUS (BYDV)
Author(s) -
Banerjee Bidisha,
Sharma Sohani Das,
Goss Dixie J.
Publication year - 2012
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.26.1_supplement.732.1
Subject(s) - eukaryotic translation , rna , biology , messenger rna , translation (biology) , eukaryotic initiation factor , fluorescence recovery after photobleaching , protein biosynthesis , eif4g , eif4a , biophysics , kinetics , microbiology and biotechnology , chemistry , physics , genetics , gene , quantum mechanics , membrane
BYDV has economic importance because it infects a broad range of cereal crops and can severely limit food grain production. Little is currently known about the mechanism of cap‐independent translation (CIT), an alternate means employed by many plant viruses e.g. BYDV to circumvent host defense mechanisms. Protein‐RNA complexes formed during the translation processes are dynamic and binding/release kinetics influence the sequential assembly of the initiation complex. The CIT mechanism was investigated by studying the role of eukaryotic initiation factors (eIF) eIF4F, eIF4B, eIF4A and PABP in the translation initiation complex formation using the biophysical techniques fluorescence anisotropy and stopped flow kinetics. BYDV translation element (BTE) located in 3’ UTR (Untranslated RNA) of mRNA and a non‐functional mutant BTEBF bound eIF4F with equal binding affinity (K d ). The presence of other eIFs had a negligible effect on the equilibrium binding of eIF4F to BTE/BTEBF RNA. Recently obtained data indicate that the BTE (first order rate constant k obs = 12.3±0.2 sec −1 ) bound eIF4F three times faster than the un‐translating BTEBF (k obs = 4.4+0.5 sec −1 ) suggesting that kinetics play a role in the translation of these RNAs.