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PMID: 8216250 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The mechanism for apo-B mRNA editing is deamination.

Biochemical and biophysical research communications ·Vol. 195 ·No. 3 ·1993-09-30 ·Pages 1204-10

Johnson DF, Poksay KS, Innerarity TL

Abstract

Apolipoprotein (apo-) B mRNA editing at nucleotide 6666 converts cytidine to uridine, transforming the codon for glutamine-2153 to a termination codon. To investigate this editing mechanism, [a-32P] and [5-3H] CTP were incorporated into synthetic apo-B RNA. After the substrate had been edited extensively in vitro by a partially purified editing extract, the edited base was isolated and analyzed for radioactivity. The uridine-6666 resulting from the editing reaction had the same ratio of 3H to 32P as did the cytidine-6666, demonstrating that deamination rather than base exchange or nucleotide replacement is the mechanism for apo-B mRNA editing.

MeSH Terms
Animals Apolipoproteins B/genetics Base Sequence Cell Separation Cell-Free System Cytidine/metabolism Deamination Epithelium/metabolism Intestine, Small/cytology,metabolism Molecular Sequence Data RNA Editing Rabbits Uridine/metabolism
Chemicals
Apolipoproteins B Cytidine Uridine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Johnson D F
Gladstone Institute of Cardiovascular Disease, University of California, San Francisco 94141-9100.
Poksay K S
Innerarity T L
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1993-09-30
Pages
1204-10
Language
English
Region
United States
NLM ID
0372516
Subset
IM
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