Disease relevance of RPS17

• A human ribosomal protein S17 cDNA [Chen et al., Proc. Natl. Acad. Sci. USA 83 (1986) 6907-6911] was used to isolate four S17 DNA clones from human genomic libraries constructed in bacteriophage lambda and cosmid vectors [1].

High impact information on RPS17

• While the overall structure of SmpB appears to be unique, the structure does contain an embedded oligonucleotide binding fold; in this respect SmpB has similarity to several other RNA-binding proteins that are known to be associated with translation, including IF1, ribosomal protein S17 and the N-terminal domain of aspartyl tRNA synthetase [2].
• RPS17 is composed of five exons and four introns that span 4 kb of DNA [1].
• Based on its transcriptional activity in a transient expression assay and on sequence similarity with S17 cDNA, cosmid clone HGS17-6 was identified as carrying the functional RPS17 gene [1].
• Two lambda clones of human genomic DNA were recognized as containing processed S17 pseudogenes, because (i) they were transcriptionally inactive in the transient assay, and (ii) they possess multiple, perfectly spliced RPS17 exons [1].
• Rapamycin-sensitive phosphorylation of ribosomal protein S17 by p70 S6 kinase [3].

Biological context of RPS17

• We demonstrate that rapamycin also inhibits the phosphorylation of another ribosomal protein identified by isolation and microsequencing as ribosomal protein S17 [3].

References