Abstract:
: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(Met)(f) 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.
journal_name
Mol Celljournal_title
Molecular cellauthors
Dallas A,Noller HFdoi
10.1016/s1097-2765(01)00356-2subject
Has Abstractpub_date
2001-10-01 00:00:00pages
855-64issue
4eissn
1097-2765issn
1097-4164pii
S1097-2765(01)00356-2journal_volume
8pub_type
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