The role of the basic N-terminal region of protein L18 in 5S RNA-23S RNA complex formation.
Of the three proteins, L5, L18 and L25, which bind to 5S RNA, the former two effect the interaction of 5S RNA with 23S RNA. We have used trypsin as a probe to investigate the roles of the proteins in this RNA-RNA assembly, with the following results: (1) In complexes with 5S RNA, the highly basic N-terminal region of L18 is accessible to trypsin. This accessibility is unaffected by L25. However, its presence is essential for stimulating L5 binding. (2) In 5S RNA-protein-23S RNA complexes proteins L5 and L18 are both strongly resistant to proteolysis. (3) No 5S RNA-23S RNA complex formation occurs in the presence of L5 and the C-terminal L18 fragment. Two possible models for the mechanism of RNA-RNA assembly are proposed.
D001426:Bacterial Proteins / Q000032:analysis*; D004926:Escherichia coli / Q000032:analysis*; D046911:Macromolecular Substances; D008970:Molecular Weight; D009698:Nucleoproteins / Q000032:analysis*; D011485:Protein Binding; D012329:RNA, Bacterial / Q000032:analysis*; D012261:Ribonucleoproteins / Q000032:analysis*; D014357:Trypsin
D001426:Bacterial Proteins; D046911:Macromolecular Substances; D009698:Nucleoproteins; D012329:RNA, Bacterial; D012261:Ribonucleoproteins; D014357:Trypsin