Author: Fredrick K. Dunny G.M. Noller H.F.
Publisher: Academic Press
ISSN: 0022-2836
Source: Journal of Molecular Biology, Vol.298, Iss.3, 2000-05, pp. : 379-394
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Abstract
Ribosomal protein S7 nucleates folding of the 16 S rRNA 3′ major domain, which ultimately forms the head of the 30 S ribosomal subunit. Recent crystal structures indicate that S7 lies on the interface side of the 30 S subunit, near the tRNA binding sites of the ribosome. To map the functional surface of S7, we have tagged the protein with a Protein Kinase A recognition site and engineered alanine substitutions that target each exposed, conserved residue. We have also deleted conserved features of S7, using its structure to guide our design. By radiolabeling the tag sequence using Protein Kinase A, we are able to track the partitioning of each mutant protein into 30 S, 70 S, and polyribosome fractions
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