Disease relevance of RPS14A

• The CRY2 gene has been isolated from a yeast genomic library cloned in bacteriophage lambda, using a CRY1 DNA probe [1].
• The predicted amino acid sequence shows that CRY1 encodes a 14,561-dalton polypeptide that has 88% amino acid sequence homology to the hamster or human S14 ribosomal protein responsible for emetine resistance and 45% homology to Escherichia coli ribosomal protein S11 [2].

High impact information on RPS14A

• Extra copies of the cry1 or RPL16 genes encoding ribosomal proteins rp59 or L16 were introduced into yeast by transformation [3].
• Several mutations within the CRY1 C terminus lead to reduced phosphorylation by phytochrome preparations in vitro [4].
• Yeast two-hybrid interaction studies using expressed C-terminal fragments of CRY1 and phytochrome A from Arabidopsis confirm a direct physical interaction between both photoreceptors [4].
• Mutations in cyh2 or cry1, producing resistance to cycloheximide and crytopleurine due to mutant ribosomal proteins, do not produce a mak- phenotype [5].
• Deletion or inactivation of CRY1 leads to 5- to 10-fold-increased levels of CRY2 mRNA [6].

Biological context of RPS14A

• Ribosomal protein 59 is an essential protein; upon sporulation of a diploid doubly heterozygous for cry1-delta 2::TRP1 cry2-delta 1::LEU2 null alleles, no spore clones containing both null alleles were recovered [1].
• The DNA sequence of the CRY2 gene contains an open reading frame encoding ribosomal protein 59 that differs at five residues from rp59 encoded by the CRY1 gene [1].
• (2) Haploids containing the cry1-delta 2::TRP1 null allele have a deficit of 40S ribosomal subunits, but cry2-delta 1::LEU2 strains have wild-type amounts of 40S ribosomal subunits [1].
• We report the sequence of a 7.5 kb region lying between the CRY1 and MAT loci of chromosome III from Saccharomyces cerevisiae [7].
• We found that the HOMOL1 and RPG consensus sequences are not necessary for the heat shock response of CRY1 [2].

Anatomical context of RPS14A

• Excess cry1 or RPL16 mRNA accumulated in polyribosomes in these cells and was translated at wild-type rates into rp59 or L16 proteins [3].

Associations of RPS14A with chemical compounds

• Reciprocal expression of RP59 and CRY1 in heterologous hosts demonstrates that glucose upshift occurs in S.cerevisiae but not K.lactis [8].
• In heterozygous (+/cry1) diploids both the sensitive and the resistant genes are expressed as shown by studies of the action of cryptopleurine on polyphenylalanine-synthesizing systems derived from each parental sensitive and resistant haploid strain and heterozygous diploid strains [9].

Other interactions of RPS14A

• These mutants were screened for pre-mRNA splicing defects by an RNA gel blot assay, using the intron- containing CRY1 and ACT1 genes as hybridization probes [10].
• The locus consists of the TRP1 and HIS3 genes inserted into chromosome III of S. cerevisiae between the CRY1 and MAT loci [11].
• The complete sequence of K3B, a 7.9 kb fragment between PGK1 and CRY1 on chromosome III, reveals the presence of seven open reading frames [12].
• The interval included the trp1 and his3 genes inserted into chromosome III of S. cerevisiae between the CRY1 and MAT loci [13].
• The segment contains two long open reading frames (ORFs): YCR591 which starts in the adjacent fragment H9G (situated towards CRY1 and the centromere), and continues with 1833 codons in YCR59 [14].

Analytical, diagnostic and therapeutic context of RPS14A

• Molecular cloning and biosynthetic regulation of cry1 gene of Saccharomyces cerevisiae [15].
• The tight linkage of the CRY1 and MAT loci, combined with the drug resistance and cell type phenotypes that they respectively control, facilitates the classification of the recombinants without resorting to tetrad dissection [11].

References