High impact information on YAR1

• We provide genetic and biochemical evidence that Yar1, a small ankyrin-repeat protein, physically interacts with RpS3, a component of the 40S subunit, and with Ltv1, a protein recently identified as a substoichiometric component of a 43S preribosomal particle [1].
• Genetic and biochemical interactions among Yar1, Ltv1 and Rps3 define novel links between environmental stress and ribosome biogenesis in Saccharomyces cerevisiae [1].
• The Yar1 ANK repeats are most similar to the conserved ANK repeats in the yeast cell cycle transcription factor, Swi6 [2].
• We show that YAR1 is not an essential gene, but that haploid cells bearing a yar1 deletion grow significantly more slowly than do isogenic wild-type cells, especially at low temperature [2].

Biological context of YAR1

• YAR1 encodes a 200-amino-acid (aa) protein with two ANK repeat motifs and an acidic C terminus rich in PEST-like sequences [2].
• YAR1 is transcribed in both haploid and diploid cells, and in haploid cells arrested in G1 with alpha-factor or in S phase with hydroxyurea [2].

Anatomical context of YAR1

• We demonstrate that cells lacking YAR1 or LTV1 are hypersensitive to particular protein synthesis inhibitors and exhibit aberrant polysome profiles, with a reduced absolute number of 40S subunits and an excess of free 60S subunits [1].

References