RRNA crosslinking

The results showed that most, if not all, proteins can be cross-linked to rRNA, suggesting that there is much rRNA in close proximity to the proteins. Studies to determine the exact sites on the rRNA which crosslink to the proteins have led to the identification of such sites for a number of proteins within both subunits (Brimacombe et al., 1983). This is illustrated for the 16 S RNA in Fig. 13 and for the 23 S RNA in Fig. 14. 

Fig. 2. The peptidyltransferase center. The structure of the central loop of Domain V of E. coli 23S rRNA is shown. Nucleotides involved in resistance against different inhibitors are indicated. Closed symbols indicate resistance and open symbols protection against chemical modification by bound antibiotic. Mutations that confer resistance to anisomycin in archaea are indicated [87] (Hcu, Halobacterium cutirubrum Hha, H. halobium). The presence of either a G or U at position 2058 in archaea is also indicated. As a consequence of this change archaea are resistant to erythromycin (Hmo, Halococcus morrhuae, Mva, Methanococcus vannielii Tte, Thermoproteus lenax Dmo, Desulfurococcus wofirfo) [29,30,88,90]. Positions where crosslinking to photoreactive derivatives of Phe-tRNA and puromycin have been observed as well as nucleotides protected by bound tRNA are also indicated. Modified from ref [73].

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