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Nucleic Acids Research, 1979, Vol. 6, No. 5 1775-1790
© 1979

Articles

RNA-protein cross-linking in Escherichia coli 30s ribosomal subunits: precise localisation of the nucleotide in 16s RNA which is coupled to protein S7 by ultraviolet irradiation

Christian Zwieb and Richard Brimacornbe

Max-Planck-Institut fur Molekulare Genetik, Abteilung Wittmann Berlin-Dahlem, GFR

Received March 6, 1979. It is well established that when E. coil 30s ribosomal subunits are irradiated with ultraviolet light under mild conditions a specific cross-link is formed between protein S7 and the 16s RNA. Methodology is presented for the analysis of the single nucleotide residue concerned in this cross-link. Firstly, the identity of the ribonuclease T1 octanucleotide attached to S7 is confirmed by a new method, which involves isolation and analysis of S7-polynucleotide complexes containing 30 – 40 nucleotides. Secondly, the isolated S7-octanucleotide complex is digested successively with ribonuclease A, proteinase K and ribonuclease T2, and the nucleotides liberated are identified. The results show unambiguously that uridine residue number 1239 in the 16s RNA sequence is cross-linked to protein S7.


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This article has been cited by other articles:


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S Stern, T Powers, L. Changchien, and H. Noller
RNA-protein interactions in 30S ribosomal subunits: folding and function of 16S rRNA
Science, May 19, 1989; 244(4906): 783 - 790.
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H. Noller and C. Woese
Secondary structure of 16S ribosomal RNA
Science, April 24, 1981; 212(4493): 403 - 411.
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