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The editing of apolipoprotein (apo)B messenger RNA (mRNA) involves a novel C to U modification, which creates an in-frame stop-translation codon, thereby generating the carboxyl-terminal of apoB48. The 27 kDa catalytic subunit of the editing enzyme has been cloned and established to be a zinc-containing cytidine deaminase. The catalytic subunit is guided to the editing site by a second targeting subunit or subunits. A candidate for the targeting subunit is a 60 kDa protein that can be UV crosslinked to the sequence UGAU, which is part of a motif downstream of the editing site that is essential for editing.

Original publication

DOI

10.1097/00041433-199404000-00004

Type

Journal article

Journal

Curr Opin Lipidol

Publication Date

04/1994

Volume

5

Pages

87 - 93

Keywords

Amino Acid Sequence, Animals, Apolipoproteins B, Base Sequence, Binding Sites, Cytidine Deaminase, Humans, Lipid Metabolism, Molecular Sequence Data, RNA Editing, RNA, Messenger, Sequence Homology