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Nucleic Acids Research, 1980, Vol. 8, No. 18 4131-4142
© 1980

MOLECULAR BIOLOGY

The role of the basic N-terminal region of protein L18 in 5S RNA–23S RNA complex formation

Veronica Newberry* and Roger A. Garrett+

Division of Biostructural Chemistry, Chemistry Department, Aarhus University DK-8000 Aarhus-C, Denmark, and Max-Planck-Institut für Molekulare Genetik, Ihnestr. 63-73, D-1000 Berlin 33, GFR

+To whom correspondence should be addressed

Received July 8, 1980.

Of the three proteins, L5, L18 and L25, which bind to 5S RNA, the former two effect the interaction of 5S RNA with 23S RNA. We have used trypsin as a probe to investigate the roles of the proteins in this RNA-RNA assembly, with the following results:

(1) In complexes with 5S RNA, the highly basic N-terminal region of L18 is accessible to trypsin. This accessibility is unaffected by L25. However, its presence is essential for stimulating L5 binding. (2) In 5S RNA-protein-23S RNA complexes proteins L5 and L18 are both strongly resistant to proteolysis. (3) No 5S RNA-23S RNA complex formation occurs in the presence of L5 and the C-terminal Ll8 fragment. Two possible models for the mechanism of RNA-RNA assembly are proposed.

*Present address: Department of Biochemistry, University of Bristol, Bristol, UK


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