Abstract
The bacterial 30S ribosomal subunit self-assembles in vitro to form an 850kDa RNP. Assembly is generally thought to advance when the core 16S rRNA navigates through many low-energy kinetic traps, guided by the 20 small-subunit proteins that recognize and lock in native RNA tertiary structure. Kinetic analyses of protein binding reveal a highly choreographed, ordered assembly process, consistent with large-scale qualitative observations of ordered protein binding and measurements of thermodynamic cooperativity within synthetic fragments of the 30S.
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