Section 9
Chapter 8,179

Apolipoprotein B mRNA editing in vitro is a zinc-dependent process

Barnes, C.; Smith, H.C.

Biochemical and Biophysical Research Communications 197(3): 1410-1414


ISSN/ISBN: 0006-291X
PMID: 8280158
DOI: 10.1006/bbrc.1993.2634
Accession: 008178791

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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.

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