| First Author | Kobayashi M | Year | 2016 |
| Journal | Sci Rep | Volume | 6 |
| Pages | 36780 | PubMed ID | 27829658 |
| Mgi Jnum | J:240459 | Mgi Id | MGI:5883637 |
| Doi | 10.1038/srep36780 | Citation | Kobayashi M, et al. (2016) The ubiquitin hybrid gene UBA52 regulates ubiquitination of ribosome and sustains embryonic development. Sci Rep 6:36780 |
| abstractText | Ubiquitination is a crucial post-translational modification; however, the functions of ubiquitin-coding genes remain unclear. UBA52 encodes a fusion protein comprising ubiquitin at the N-terminus and ribosomal protein L40 (RPL40) at the C-terminus. Here we showed that Uba52-deficient mice die during embryogenesis. UBA52-deficient cells exhibited normal levels of total ubiquitin. However, UBA52-deficient cells displayed decreased protein synthesis and cell-cycle arrest. The overexpression of UBA52 ameliorated the cell-cycle arrest caused by UBA52 deficiency. Surprisingly, RPL40 expression itself is insufficient to regulate cyclin D expression. The cleavage of RPL40 from UBA52 was required for maintaining protein synthesis. Furthermore, we found that RPL40 formed a ribosomal complex with ubiquitin cleaved from UBA52. UBA52 supplies RPL40 and ubiquitin simultaneously to the ribosome. Our study demonstrated that the ubiquitin-coding gene UBA52 is not just an ubiquitin supplier to the ubiquitin pool but is also a regulator of the ribosomal protein complex. These findings provide novel insights into the regulation of ubiquitin-dependent translation and embryonic development. |
