Abstract
Zinc finger motifs are common in ribosomal proteins: they are widely distributed in nature, having been found amongst the proteins of both subunits of the ribosomes of all species examined in the three kingdoms; the motif is always of the C2C2 variety and occurs only once in a protein. Despite wide distribution there is neither strict conservation of the ribosomal proteins with the motif nor of the entire motif in homologous proteins. A comprehensive genetic, biochemical, and structural analysis has been made of the contribution of the zinc finger to the function of yeast ribosomal protein YL37a, to date the only study of its kind. Replacement, one at a time, of the cysteines with serines in the motif in YL37a revealed that all four cysteines are required for the binding of zinc; nonetheless, cells with mutations in three of the four cysteines do not suffer a significant impairment of growth, nor is the binding to rRNA of the mutant proteins materially affected. It is possible that the zinc finger motif in ribosomal proteins are the vestiges, biological fossils if you will, of a former function, and that the motif has been preserved despite the ribosomal proteins having come to use alternate amino acid sequences and/or structures to bind to rRNA as has been shown to be the case for YL37a.
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Dresios, J., Chan, YL., Wool, I.G. (2005). Ribosomal Zinc Finger Proteins: The Structure and the Function of Yeast YL37a. In: Iuchi, S., Kuldell, N. (eds) Zinc Finger Proteins. Molecular Biology Intelligence Unit. Springer, Boston, MA. https://doi.org/10.1007/0-387-27421-9_14
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DOI: https://doi.org/10.1007/0-387-27421-9_14
Publisher Name: Springer, Boston, MA
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