A novel RNA-binding motif in omnipotent suppressors of translation termination, ribosomal proteins and a ribosome modification enzyme?
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 protein 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.
Koonin
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National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894.
Bork
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Sander
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D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry; D004926:Escherichia coli / Q000235:genetics; D005656:Fungal Proteins / Q000737:chemistry; D006801:Humans; D008969:Molecular Sequence Data; D014176:Protein Biosynthesis; D012313:RNA / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry*; D012269:Ribosomal Proteins / Q000737:chemistry; D012270:Ribosomes / Q000378:metabolism
D001426:Bacterial Proteins; D005656:Fungal Proteins; D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins; D012313:RNA