Function of the repeating homologous sequences in nucleic acid binding domain of ribosomal protein S1.
Ribosomal protein S1 contains in its RNA binding domain four repeating, homologous stretches of sequences. Its functionally active mutant form m1-S1 [Subramanian, A.R., & Mizushima, S. (1979) J. Biol. Chem. 254, 4309] contains only three repeating stretches. In order to assess the functional importance of this repeating sequence, we cleaved S1 at its reactive SH group on Cys-349 and isolated a fragment (S1-F4) that has lost two of the homologous stretches but retains all other essential elements. We find that ribosomes reconstituted with S1-F4 instead of S1 are functionally active in translating poly(U) and poly(A) but totally inactive in translating phage MS2 RNA. The significance of this result is discussed vis-à-vis the initiation step in translating natural mRNA, and a functional role for the tetrarepeat of S1 is suggested.
D000595:Amino Acid Sequence; D001665:Binding Sites; D003553:Cystine / Q000032:analysis; D004926:Escherichia coli; D005779:Immunodiffusion; D010446:Peptide Fragments / Q000302:isolation & purification; D012329:RNA, Bacterial / Q000378:metabolism; D012269:Ribosomal Proteins / Q000032:analysis* / Q000378:metabolism
D010446:Peptide Fragments; D012329:RNA, Bacterial; D012269:Ribosomal Proteins; C015494:ribosomal protein S1; D003553:Cystine