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Nucleic Acids Research, 1994, Vol. 22, No. 11 2166-2167
© 1994

RNA

A novel RNA-binding motif in omnipotent suppressors of translation termination, ribosomal proteins and a ribosome modification enzyme?

Eugene V. Koonin*,, Peer Bork1,2 and Chris Sander1

National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health Bethesda, MD 20894, USA 1Molecular Biology Laboratory Meyerhofstrasse 1, D-69012 Heidelberg 2Max-Delbruck-Center for Molecular Medicine D-13189 Berlin, Germany

* To whom correspondence should be addressed

Received March 15, 1994. Accepted April 25, 1994.

Using computer methods for database search, multiple alignment, protein sequence motif analysis and secondary structure prediction, a putative new RNA-binding motif was identified. The novel motif is conserved in yeast omnipotent translation termination suppressor SUP1, the related DOM34 protein and its pseudogene homologue; three groups of eukaryotic and archaeal ribosomal proteins, namely L30e, L7Ae/S6e and S12e; an uncharacterized Bacillus subtilis protien related to the L7A/S6e group; and Escherichia coli ribosomal protein modification enzyme RimK. We hypothesize that a new type of RNA-binding domain may be utilized to deliver additional activities to the ribosome.


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