Understanding translation at the molecular level depends upon understanding the three-dimensional structure of the ribosome. The purpose of this proposal is to map the three-dimensional proximities between 16S rRNA and specific sites within certain 30S ribosomal proteins. A modification of hydroxyl radical cleavage, using tethered Fe(II)-EDTA, will generate an extensive set of unambiguous constraints for the folding of 16S rRNA in a fully reconstituted 30S ribosomal subunit.
Culver, G M; Cate, J H; Yusupova, G Z et al. (1999) Identification of an RNA-protein bridge spanning the ribosomal subunit interface. Science 285:2133-6 |
Culver, G M; Heilek, G M; Noller, H F (1999) Probing the rRNA environment of ribosomal protein S5 across the subunit interface and inside the 30 S subunit using tethered Fe(II). J Mol Biol 286:355-64 |
Culver, G M; Noller, H F (1999) Efficient reconstitution of functional Escherichia coli 30S ribosomal subunits from a complete set of recombinant small subunit ribosomal proteins. RNA 5:832-43 |