Ribosomal Protein S27 Like Protein (RPS27L)

RPS27L shares 96.3% amino acid identity with RPS27. Expression of RPS27L was detected in most human tissues and human cancer cell lines examined.

Gel retardation and chromatin immunoprecipitation assays showed that p53 bound to a putative p53-binding site in RPS27L intron 1. p53 activated transcription of a reporter gene driven by the RPS27L intron 1 sequence, and etoposide, a DNA-damaging agent that upregulates p53 expression, increased expression of the reporter gene. RPS27L expression promoted apoptosis following etoposide exposure, whereas small interfering RNA against RPS27L inhibited etoposide-induced apoptosis. p53 induces expression of RPS27L, which in turn promotes apoptosis.