Apolipoprotein B mRNA editing in vitro is a zinc-dependent process.
Apolipoprotein B mRNA editing involves the conversion of a cytidine at nucleotide 6666 to a uridine, thereby creating a translational stop codon from a glutamine codon. Recent evidence suggest that a cytidine deaminase is responsible for catalyzing the C to U conversion. All known nucleotide deaminases require zinc as part of their catalytic domain. Utilizing the selective chelator for zinc, 1,10-penanthroline, we demonstrate that in vitro editing activity in rat liver extracts is zinc dependent. These data, taken together with recent reports, strongly support a role for a cytidine deaminase and nucleotide conversion as the catalytic mechanism for apoB mRNA editing.
Barnes
C
C
Department of Biochemistry, University of Rochester, NY 14642.
Smith
H C
HC
D000818:Animals; D001055:Apolipoproteins B / Q000096:biosynthesis*; D002467:Cell Nucleus / Q000378:metabolism*; D003564:Cytidine Deaminase / Q000378:metabolism; D007502:Iron Chelating Agents / Q000494:pharmacology; D008099:Liver / Q000187:drug effects / Q000378:metabolism*; D010618:Phenanthrolines / Q000494:pharmacology; D012333:RNA, Messenger / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats; D012492:Salts / Q000494:pharmacology; D015032:Zinc / Q000378:metabolism / Q000494:pharmacology*
D001055:Apolipoproteins B; D007502:Iron Chelating Agents; D010618:Phenanthrolines; D012333:RNA, Messenger; D012492:Salts; D003564:Cytidine Deaminase; D015032:Zinc; C025205:1,10-phenanthroline