| First Author | Dance GS | Year | 2001 |
| Journal | Nucleic Acids Res | Volume | 29 |
| Issue | 8 | Pages | 1772-80 |
| PubMed ID | 11292850 | Mgi Jnum | J:68869 |
| Mgi Id | MGI:1933652 | Doi | 10.1093/nar/29.8.1772 |
| Citation | Dance GS, et al. (2001) Identification of the yeast cytidine deaminase CDD1 as an orphan C-->U RNA editase. Nucleic Acids Res 29(8):1772-80 |
| abstractText | Yeast co-expressing rat APOBEC-1 and a fragment of human apolipoprotein B (apoB) mRNA assembled functional editosomes and deaminated C6666 to U in a mooring sequence-dependent fashion. The occurrence of APOBEC-1-complementing proteins suggested a naturally occurring mRNA editing mechanism in yeast. Previously, a hidden Markov model identified seven yeast genes encoding proteins possessing putative zinc-dependent deaminase motifs. Here, only CDD1, a cytidine deaminase, is shown to have the capacity to carry out C-->U editing on a reporter mRNA. This is only the second report of a cytidine deaminase that can use mRNA as a substrate. CDD1-dependent editing was growth phase regulated and demonstrated mooring sequence-dependent editing activity. Candidate yeast mRNA substrates were identified based on their homology with the mooring sequence-containing tripartite motif at the editing site of apoB mRNA and their ability to be edited by ectopically expressed APOBEC-1. Naturally occurring yeast mRNAs edited to a significant extent by CDD1 were, however, not detected. We propose that CDD1 be designated an orphan C-->U editase until its native RNA substrate, if any, can be identified and that it be added to the CDAR (cytidine deaminase acting on RNA) family of editing enzymes. |
