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Nucleic Acids Research, 1989, Vol. 17, No. 10 3757-3762
© 1989

MOLECULAR BIOLOGY

Ribosomal protein L7/L12 has a helix-turn-helix motif similar to that found in DNA-binding regulatory proteins

Phoebe A. Rice and Thomas A. Steitz

Department of Molecular Biophysics and Biochemistry and Howard Hughes Medical Institute, Yale University New Haven, CT 06511, USA

Received January 23, 1989. Revised April 17, 1989. Accepted April 17, 1989.

Inspection of the structure of the C-terminal domain of ribosomal protein L7/L12 (1) reveals a helix-turn-helix motif similar to the one found in many DNA-binding regulatory proteins (2–5). The 19 {alpha}-carbon atoms of the L7/L12 {alpha}-helices superimpose on the DNA binding helices of CAP and cro with root-mean-square distances between corresponding alpha carbons of 1.45 and 1.55 Å, respectively. These helices in L7/L12 are within a patch of highly conserved residues on the surface of L7/L12 whose role is as yet uncertain. We raise the possibility that they may constitute a binding site for nucleic acids, most probably RNA. Consistent with this hypothesis are calculations of the electrostatic charge potential surrounding the protein, which show a region of positive potential centered on the first of these helices.


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