Identification of the yeast cytidine deaminase CDD1 as an orphan C-->U RNA editase.

Abstract:

: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.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Dance GS,Beemiller P,Yang Y,Mater DV,Mian IS,Smith HC

doi

10.1093/nar/29.8.1772

keywords:

subject

Has Abstract

pub_date

2001-04-15 00:00:00

pages

1772-80

issue

8

eissn

0305-1048

issn

1362-4962

journal_volume

29

pub_type

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