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Nucleic Acids Research, 1988, Vol. 16, No. 3 815-832
© 1988

Articles

RNA-protein cross-linking in Escherichia coli 50S ribosontal subunits; determination of sites on 23S RNA that are cross-linked to proteins L2, L4, L24 and L27 by treatment with 2-iminothiolane

Heinz Gulle1, Edmund Hoppe2, Monika Osswald, Barbara Greuer, Richard Brimacombe* and Georg Stöffler+

Max-Plank-Institut für Molekulare Genetik Abteilung Wittmann, D-1000 Berlin-Dahlem, FRG +Institut für Mikrobiologie, Medizinische Fakultät, Universität Innsbruck A-6020 Innsbruck, Austria

*To whom correspondence should be addressed

Received December 15, 1987. Accepted January 11, 1988.

RNA-protein cross-links were introduced into E. coli 50S ribosomal subunits by treatment with 2-iminothiolane followed by mild ultraviolet irradiation. After partial digestion of the RNA, the cross-linked RNA-protein complexes were separated by our recently published three-step procedure. In cases where this separation was inadequate, a further purification step was introduced, involving affinity chromatography with antibodies to the ribosomal 50S proteins. Analysis of the isolated complexes enabled four new cross-link sites on the 23S RNA to be identified, as well as re-confirming several previously established sites. The new sites are as follows: Protein L2 is cross-linked within an oligonucleotide at positions 1818–1823 in the 23S RNA, protein L4 within positions 320–325, protein L24 within positions 99–107, and protein L27 within positions 2320–2323.

1Universität Ulm, Abteilung Mikrobiologie und Immunologie, D-7900 Ulm

2Max-Planck-Institut für Biochemie, D-8033 Martinsried bei München, FRG


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