{'fraction_non_alphanumeric': 0.026449643947100712, 'fraction_numerical': 0.01627670396744659, 'mean_word_length': 5.0, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
An extremely high conservation of RNA‐protein S7 interactions during prokaryotic ribosomal biogenesis

Direct determination of RNA‐protein complex structures is often facilitated by the use of thermophilic proteins; however E.coli is the most investigated system so far. A hybrid approach is to form heterologous complexes of E.coli RNA with thermophitic proteins. The rationale for this approach to RNA‐protein interactions in ribosomes is based on the ability of the thermophilic protein S7 to replace a homologous counterpart in vivo. In vitro, the protein S7 of Thermus thermophilus is able to form complexes with both the minimal 16S rRNA fragment and the intercistronic region of the str operon mRNA from E.coli (Kd=1.4×10‐7 M and 1.1×l0‐7 M respectively). The interaction of Thermus S7 with the E. coli intercistronic mRNA is surprising, because this region does not exist in the thermophilic str operon. It suggests a high degree of conservation of an RNA‐binding site on S7.