Disease relevance of RPL28

• The complete amino acid sequences of the ribosomal proteins L25, L29 and L31 were established by analyses of the peptides obtained by enzymatic digestion with trypsin, Staphylococcus aureus protease, chymotrypsin and lysylendopeptidase [1].

High impact information on RPL28

• Northern blot analysis revealed the disappearance of some mRNAs (CYH2 and HIS4) consistent with a role for poly(A) tails in mRNA stability [2].
• In L29 the corresponding Arg 25----Lys substitution within the nuclear localizing sequence distal to the N-terminus was without effect, as evidence by normal rates of ribosome assembly and cell growth [3].
• Mixing and matching of the elements from the ACT1 and CYH2 gene introns showed that these elements can cooperate in an intron-specific fashion to control spliceosome assembly [4].
• Mutations in the yeast ribosomal protein L29 gene (CYH2) are known that confer cycloheximide resistance [5].
• The L27' cDNA was expressed in yeast to determine the ability of the mouse protein to substitute for yeast L29 in assembling a functional ribosome [6].

Biological context of RPL28

• Along with three novel ORFs, encoding two proteins of unknown molecular function and one putative hexose transporter, this segment also contained the Kl-RPL28 gene, found to be responsible for the cycloheximide resistance of heterologous transformants [7].
• Mutations in cyh2 or cry1, producing resistance to cycloheximide and crytopleurine due to mutant ribosomal proteins, do not produce a mak- phenotype [8].
• Mutations in ICK1 restore kinetochore function but have no effect on ctf13-30 mRNA or CYH2 pre-mRNA accumulation [9].
• In order to define the cis -acting element(s) of ribosomal protein genes sensitive to a defect in the secretory pathway, we have constructed a series of fusion genes containing the CYH2 promoter region, with various deletions, fused to lacZ [10].
• Structural analysis of the recombinant plasmids obtained from the resistant cells showed that the plasmids had deletions at various sites of the CAN1-CYH2 region and there were only short regions of homology (1-5 bp) at the recombination junctions [11].

Anatomical context of RPL28

• A significant fraction of the CYH2 pre-mRNA that accumulated in the presence of cycloheximide was associated with polysomes, but disappeared from that fraction when decay resumed in the absence of the drug [12].

Associations of RPL28 with chemical compounds

• Upon formation of a deletion over the active CAN1-CYH2 genes, a cell becomes resistant to both canavanine and cycloheximide [13].
• Yeast cells unable to transcribe tcm1 or cyh2 without galactose did not grow [14].
• (1) we find that resistance to cycloheximide is due to a transversion mutation resulting in the replacement of a glutamine by glutamic acid in position 37 of L29 [15].
• Intron mutations that affect the splicing efficiency of the CYH2 gene of Saccharomyces cerevisiae [16].
• The left arm of chromosome VII carries a tightly centromere linked marker, leu1 (leucine requirement), distal to leu1 in this order: trp5 (tryptophan requirement), cyh2 (recessive resistance to cycloheximide) and met 13 (requirement for methionine) [17].

Enzymatic interactions of RPL28

• A diploid strain of the yeast Saccharomyces cerevisiae has been constructed that has one copy of the ribosomal protein gene CYH2 completely deleted and replaced with the TRP1 gene using the method of Rothstein (1983) [18].

Regulatory relationships of RPL28

• This strain also contains the wild-type CYH2 allele under the transcriptional control of the Gal1 promoter [19].

Other interactions of RPL28

• We placed a regulatory sequence derived from the GAL10 locus of Saccharomyces cerevisiae at various distances from the start sites of transcription of two yeast ribosomal protein genes, tcm1 and cyh2 [14].
• First, an internal region of the cloned HIS3 gene was replaced by a DNA segment containing the wild-type ribosomal protein gene, CYH2 [20].
• Effects of progressive depletion of TCM1 or CYH2 mRNA on Saccharomyces cerevisiae ribosomal protein accumulation [21].
• The second fragment covers the 72.6 kb region between the chromosomal markers CYH2 and ALG2 [22].
• It shows 80.4% homology to protein L29 from the large ribosomal subunit of rat and is related to yeast YL43 [23].

Analytical, diagnostic and therapeutic context of RPL28

• Molecular cloning and analysis of yeast gene for cycloheximide resistance and ribosomal protein L29 [24].
• Tetrad dissection shows that haploid spores lacking the CYH2 gene cannot germinate [18].

References