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. 1978 Aug;5(8):2789–2799. doi: 10.1093/nar/5.8.2789

On the role of protein S4 N-terminal residues 1 through 30 in 30S ribosome function.

L M Changchien, J Schwarzbauer, M Cantrell, G R Craven
PMCID: PMC342207  PMID: 358148

Abstract

30S ribosomal protein S4 contains a single cysteine residue at position 31. We have selectively cleaved the peptide bond adjacent to this residue using the reagent 2-nitro-5-thiocyanobenzoic acid. The two resultant fragments were purified. The smaller S4-fragment (1-30) was found to be incapable of interacting with 16S RNA directly. This fragment also is not incorporated into a particle reconstituted from 16S RNA and 20 purified proteins with S4 missing. In contrast, the large S4-fragment (31-203) appears to be fully functional in ribosome assembly. Replacement of S4 with this fragment in the reconstitution reaction leads to a complete 30S ribosome containing all 30S proteins. This particle has a full capacity to bind poly U but has lost all activity for poly U directed phe-tRNA binding. We therefore propose that the N-terminus of protein S4 is not critical for ribosome assembly but is essential for tRNA binding.

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Selected References

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