Journal
MOLECULAR CELL
Volume 22, Issue 1, Pages 105-115Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2006.02.014
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Funding
- NIGMS NIH HHS [R01 GM065265-03] Funding Source: Medline
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Translation initiation is a key step for regulating the level of numerous proteins within the cell. In bacteria, the 30S initiation complex directly binds to the translation initiation region (TIR) of the mRNA. How the ribosomal 30S subunit assembles on highly structured TIR is not known. Using fluorescence-based experiments, we assayed 12 different mRNAs that form secondary structures with various stabilities and contain ShineDalgarno (SD) sequences of different strengths. A strong correlation was observed between the stability of the mRNA structure and the association and dissociation rate constants. Interestingly, in the presence of initiation factors and initiator tRNA, the association kinetics of structured mRNAs showed two distinct phases. The second phase was found to be important for unfolding structured mRNAs to form a stable 30S initiation complex. We show that unfolding of structured mRNAs requires a SD sequence, the start codon, fMet-tRNA(fmet), and the GTP bound form of initiation factor 2 bound to the 30S subunit.
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