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Nucleic Acids Research, 1993, Vol. 21, No. 21 4936-4940
© 1993

MOLECULAR BIOLOGY

Ribosomal protein L25 from Trypanosoma brucei: phytogeny and molecular co-evolution of an rRNA-binding protein and its rRNA binding site

Stan Metzenberg, Christine Joblet, Philippe Verspieren and Nina Agabian

Intercampus Program in Molecular Parasitology, University of California San Francisco, San Francisco, CA 94143-1204, USA

Received July 14, 1993. Revised September 17, 1993. Accepted September 17, 1993.

The gene encoding ribosomal protein L25, a primary rRNA-binding protein, was isolated from the protozoan parasite Trypanosoma brucei. Hybridization studies indicate that multiple copies of the gene are present per T.brucei haploid genome. The C-terminal domain of L25 protein from T.brucei is strikingly similar to L23a protein from rat, L25 proteins from fungal species, and L23 proteins from eubacteria, archaebacteria, and chloroplasts. A phylogenetic analysis of L23/25 proteins and the putative binding sites on their respective LSU-rRNAs (large subunit rRNAs) provides a rare opportunity to study molecular co-evolution between an RNA molecule and the protein that binds to it.


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