Journal
MOLECULAR CELL
Volume 8, Issue 4, Pages 855-864Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(01)00356-2
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Funding
- NIGMS NIH HHS [GM 59140, GM 17129, F32 GM 20108-01] Funding Source: Medline
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Hydroxyl radical footprinting and directed probing from Fe(II)-derivatized IF3 have been used to map the interaction of IF3 relative to 16S rRNA and tRNA(f)(Met) in the 30S ribosomal subunit. Our results place the two domains of IF3 on opposite sides of the initiator tRNA, with the C domain at the platform interface and the N domain at the E site. The C domain coincides with the location of helix 69 of 23S rRNA, explaining the ability of IF3 to block subunit association. The N domain neighbors proteins S7 and S11 and may interfere with E site tRNA binding. Our model suggests that IF3 influences initiator tRNA selection indirectly.
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