Localisation of part of the binding sites of 30S ribosomal proteins S4 and S20 in a small uninterrupted fragment of 16S RNA.
Analyses of the T1 ribonuclease-alkaline phosphatase fingerprint of a continuous fragment of the 16S rRNA, 170-230 nucleotides long, isolated from the products of autodigestion of 30S ribosome subunits show that it contains a sequence near the 5'-phosphate terminus of intact 16S rRNA and corresponds to segment H'-M of this molecule as defined by Ehresmann et al [29]. Incubation of this fragment with total 30S ribosomal proteins under reconstitution conditions leads to the formation of a complex containing proteins S4, S20, and one or both of proteins S16 and S17. The stoichiometry of these proteins in the complex is discussed.
D000469:Alkaline Phosphatase; D004926:Escherichia coli / Q000378:metabolism; D008970:Molecular Weight; D011485:Protein Binding; D012335:RNA, Ribosomal / Q000378:metabolism; D006163:Ribonuclease T1; D012269:Ribosomal Proteins / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism
D012335:RNA, Ribosomal; D012269:Ribosomal Proteins; D006163:Ribonuclease T1; D000469:Alkaline Phosphatase