A case of convergent evolution of nucleic acid binding modules
- 1 April 1996
- Vol. 18 (4) , 309-315
- https://doi.org/10.1002/bies.950180409
Abstract
Divergent evolution can explain how many proteins containing structurally similar domains, which perform a variety of related functions, have evolved from a relatively small number of modules or protein domains. However, it cannot explain how protein domains with similar, but distinguishable, functions and similar, but distinguishable, structures have evolved. Examples of this are the RNA‐binding proteins containing the RNA‐binding domain (RBD), and a newly established protein group, the cold‐shock domain (CSD) protein family. Both protein domains contain conserved RNP motifs on similar single‐stranded nucleic acid‐binding surfaces. Apart from the RNP motifs, which have a similar function, the two families show little similarity in topology or amino acid sequence. This can be considered an interesting example of convergent evolution at the molecular level. Previously, a β‐sheet surface was found to interact with RNA in non‐homologous proteins from yeast, phage and man, revealing that this mode of RNA binding may be a widely recurring theme.Keywords
This publication has 49 references indexed in Scilit:
- Mutational analysis of the putative nucleic acid‐binding surface of the cold‐shock domain, CspB, revealed an essential role of aromatic and basic residues in binding of single‐stranded DNA containing the Y‐box motifMolecular Microbiology, 1995
- An RBD that does not bind RNA: NMR secondary structure determination and biochemical properties of the C-terminal RNA binding domain from the human U1A proteinJournal of Molecular Biology, 1995
- Solution structure of the active domain of tissue inhibitor of metalloproteinases-2. A new member of the OB fold protein familyBiochemistry, 1994
- Structural and functional properties of the evolutionarily ancient Y‐box family of nucleic acid binding proteinsBioEssays, 1994
- DNA supercoiling and thermal regulation of unsaturated fatty acid synthesis in Bacillus subtilisMolecular Microbiology, 1994
- The major cold shock protein of Bacillus subtilis CspB binds with high affinity to the ATTGG‐ and CCAAT sequences in single stranded oligonucleotidesFEBS Letters, 1994
- Interaction of the main cold shock protein CS7.4 (CspA) of Escherichia coli with the promoter region of hnsBiochimie, 1994
- Convergent evolution: the need to be explicitTrends in Biochemical Sciences, 1994
- Ribosomal protein S17: Characterization of the three-dimensional structure by proton and nitrogen-15 NMRBiochemistry, 1993
- Proton, carbon-13, and nitrogen-15 NMR assignments and global folding pattern of the RNA-binding domain of the human hnRNP C proteinsBiochemistry, 1992