| First Author | Belhumeur P | Year | 1987 |
| Journal | Nucleic Acids Res | Volume | 15 |
| Issue | 3 | Pages | 1019-29 |
| PubMed ID | 2434927 | Mgi Jnum | J:8614 |
| Mgi Id | MGI:57079 | Doi | 10.1093/nar/15.3.1019 |
| Citation | Belhumeur P, et al. (1987) Isolation and characterisation of a murine cDNA clone highly homologous to the yeast L29 ribosomal protein gene. Nucleic Acids Res 15(3):1019-29 |
| abstractText | We report here the isolation of a murine cDNA clone (cCL3) which is homologous to the mRNA of the yeast ribosomal protein L29. Comparison of the deduced amino-acid composition of cCL3 to those known for rat ribosomal proteins indicates that this cDNA codes for mammalian ribosomal protein L27'. The gene corresponding to the cDNA is present at approximately 15 copies per genome, some of these probably representing processed pseudogenes. The cDNA hybridizes to an mRNA of 600 nucleotides from various mammals at high stringency, and to an avian transcript of the same size at low stringency. It has been suggested that L29 is involved in peptidyl transferase activity. The strong homology of mammalian L27' to yeast L29 suggests a function which has been conserved throughout evolution, and thus L27' may also be involved in peptidyl transferase activity. |
