부산대학교 도서관

Ribosomal proteins (RPs) are essential components of ribosomes, but several RPs are also present at transcription sites of eukaryotic chromosomes. Here, we report a genome-wide ChIP-on-chip analysis of the association of three representative 60S RPs with sites in the Schizosaccharomyces pombe chromosomes. All three proteins tend to bind at the same subset of coding and noncoding loci. The data demonstrate selective RNA-dependent interactions between RPs and many transcription sites and suggest that the RPs bind as components of a preassembled multiprotein complex, perhaps 60S or pre-60S subunits. These findings further indicate that the presence of RPs complexes at transcription sites might be a general feature of eukaryotic cells and functionally important. Unexpectedly, the RPs' chromosomal association is highest at centromeres and tRNA genes—the RPs were found at 167 of the 171 tRNA genes assayed. These findings raise the intriguing possibility that RP complexes are involved in tRNA biogenesis and possibly centromere functions.