| Popis: |
In the early 1980s, it was recognized that the equimolar accumulation of ribosomal proteins (r-proteins) in eukaryotes is maintained by coordinated regulation at various levels of gene expression, from transcription to protein stability. With the possible exception of yeast, the translational control of mRNA utilization emerged to be the prevalent regulatory mechanism involved. It was also soon realized that the corresponding r-protein genes share a common architecture, mainly in the region surrounding the 5´ end, that was found to be involved in the coregulated expression of gene activity at the transcriptional and translational levels. As described below the most typical common structural feature is the transcription initiation site which is always situated within a 12–25 pyrimidine tract flanked by regions of high G + C content. |
