RNA binding to APOBEC deaminases; Not simply a substrate for C to U editing.

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Smith HC

RNA binding to APOBEC deaminases; Not simply a substrate for C to U editing.

RNA Biol. 2017 Sep 2;14(9):1153-1165. doi: 10.1080/15476286.2016.1259783. Epub 2016 Nov 21.

PubMed ID

27869537 [ View in PubMed

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Abstract

Apolipoprotein B mRNA Editing Catalytic Polypeptide-like 1 or APOBEC1 was discovered in 1993 as the zinc-dependent cytidine deaminase responsible for the production of an in frame stop codon in apoB mRNA through modification of cytidine at nucleotide position 6666 to uridine. At the time of this discovery there was much speculation concerning the mechanism of base modification RNA editing which has been rekindled by the discovery of multiple C to U RNA editing events in the 3' UTRs of mRNAs and the finding that other members of the APOBEC family while able to bind RNA, have the biological function of being DNA mutating enzymes. Current research is addressing the mechanism for these nucleotide modification events that appear not to adhere to the mooring sequence-dependent model for APOBEC1 involving the assembly of a multi protein containing editosome. This review will summarize our current understanding of the structure and function of APOBEC proteins and examine how RNA binding to them may be a regulatory mechanism.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Zinc chloride	C->U-editing enzyme APOBEC-1	Protein	Humans	Unknown	Cofactor Chelator	Details
Zinc sulfate, unspecified form	C->U-editing enzyme APOBEC-1	Protein	Humans	Unknown	Cofactor Chelator	Details