An NMR study of the helix V-loop E region of the 5S RNA from Escherichia coli.
Experiments are described that complete the assignment of the imino proton NMR spectrum of the fragment 1 domain from the 5S RNA of Escherichia coli. Most of the new assignments fall in the helix V-loop E portion of the molecule (bases 70-78 and 98-106), the region most sensitive to the binding of ribosomal protein L25. The spectroscopic data are incompatible with the standard, phylogenetically derived model for 5S RNA, which makes all the base pairs possible in loop E with the sequences aligned in parallel (C70-G106, C71-G105, etc.) [see Delihas et al. (1984) Prog. Nucleic Acid Res. Mol. Biol. 31, 161-190]. Furthermore, the alternative loop E model proposed for spinach chloroplast 5S RNA by Romby et al. [(1988) Biochemistry 27, 4721-4730] does not apply to the closely homologous 5S RNA from E. coli. The 5S RNAs from E. coli and spinach chloroplasts do not have the same secondary structures in solution despite their strong sequence homologies, and neither appears to conform to the standard model for 5S RNA in the loop E region.
Zhang
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Department of Chemistry, Yale University, New Haven, Connecticut 05611.
Moore
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PB
D002736:Chloroplasts / Q000032:analysis; D004926:Escherichia coli / Q000032:analysis / Q000235:genetics*; D009682:Magnetic Resonance Spectroscopy; D008954:Models, Biological; D009154:Mutation; D009690:Nucleic Acid Conformation; D010446:Peptide Fragments / Q000032:analysis; D010945:Plants, Edible / Q000032:analysis; D010957:Plasmids; D012335:RNA, Ribosomal / Q000032:analysis*; D012341:RNA, Ribosomal, 5S / Q000032:analysis*; D012269:Ribosomal Proteins / Q000032:analysis; D012689:Sequence Homology, Nucleic Acid
D010446:Peptide Fragments; D012335:RNA, Ribosomal; D012341:RNA, Ribosomal, 5S; D012269:Ribosomal Proteins; C031127:ribosomal protein L25