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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. [References: 31]

Type

Journal article

Publication Date

1994

Volume

5

Pages

87 - 93

Keywords

Amino Acid Sequence Animal *Apolipoproteins B/ge [Genetics] Base Sequence Binding Sites Cytidine Deaminase/ch [Chemistry] *Cytidine Deaminase/me [Metabolism] Human Lipids/me [Metabolism] Molecular Sequence Data *RNA Editing RNA, Messenger/ch [Chemistry] *RNA, Messenger/me [Metabolism] Sequence Homology Review