Reference: Tang BZ and Nazar RN (1991) Structure of the yeast ribosomal 5 S RNA-binding protein YL3. J Biol Chem 266(10):6120-3

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Abstract


A gene coding for the 5 S rRNA-binding protein (YL3) in yeast (Saccharomyces cerevisiae) was isolated using a polymerase chain reaction-amplified gene probe. The DNA sequence contains no introns and codes for a 297 amino acid (Mr = 33,741) protein. Although the protein is just 1 residue longer than in rat, unlike the high sequence homology in the 5 S rRNAs from the same organisms, only about 45% of the amino acid residues are conserved with surprisingly little homology in the carboxyl-terminal end. Nevertheless, comparative studies indicate that a number of structural features are conserved including small repeats in the primary structure and a number of helical estimates in the higher order structure. One of the sequence repeats also appears to be present in the carboxyl-terminal end of the eukaryotic transcription factor TFIIIA suggesting an evolutionary relationship in these 5 S RNA-binding proteins.

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Journal Article | Research Support, Non-U.S. Gov't
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Tang BZ, Nazar RN
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