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Reference: Cardenas D, et al. (2012) P1 and P2 protein heterodimer binding to the P0 protein of Saccharomyces cerevisiae is relatively non-specific and a source of ribosomal heterogeneity. Nucleic Acids Res 40(10):4520-9

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Abstract

The ribosomal stalk is formed by four acidic phosphoproteins in Saccharomyces cerevisiae, P1a, P1?, P2a and P2?, which form two heterodimers, P1a/P2? and P1?/P2a, that preferentially bind to sites A and B of the P0 protein, respectively. Using mutant strains carrying only one of the four possible P1/P2 combinations, we found a specific phenotype associated to each P1/P2 pair, indicating that not all acidic P proteins play the same role. The absence of one P1/P2 heterodimer reduced the rate of cell growth by varying degrees, depending on the proteins missing. Synthesis of the 60S ribosomal subunit also decreased, particularly in strains carrying the unusual P1a-P2a or P1?-P2? heterodimers, although the distinct P1/P2 dimers are bound with similar affinity to the mutant ribosome. While in wild-type strains the B site bound P1?/P2a in a highly specific manner and the A site bound the four P proteins similarly, both the A and B binding sites efficiently bound practically any P1/P2 pair in mutant strains expressing truncated P0 proteins. The reported results support that while most ribosomes contain a P1a/P2?-P0-P1?/P2a structure in normal conditions, the stalk assembly mechanism can generate alternative compositions, which have been previously detected in the cell.

Reference Type
Journal Article
Authors
Cardenas D, Revuelta-Cervantes J, Jimenez-Diaz A, Camargo H, Remacha M, Ballesta JP
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