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pubmed:abstractText |
Using derivatives of oligoribonucleotides bearing an active group at the 5'- or 3'-end, the affinity modification of Escherichia coli ribosomes has been investigated in model complexes imitating various steps of initiation and elongation with a different extent of approximation to the real protein-synthesizing system. The protein environment of the ribosome decoding site is determined. The S3, S4, S9, L2, L7/L12 proteins belong to the 5'-region of the decoding site, and the S5, S7, S9, L1, L16 proteins to the 3'-region. In the process of translation the template moves along the external side of the 30 S subunit, from the L1 ridge to the L7/L12 stalk. The structural arrangement of the decoding site or its nearest environment depends on the functional state of ribosomes in the process of translation.
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