RNA editing-associated protein 1 is an RNA binding protein with specificity for preedited mRNA.

Abstract:

:RNA editing in the mitochondria of kinetoplastids involves the addition and deletion of uridines at specific sites as directed by guide RNAs (gRNAs). Ample evidence shows that ribonucleoprotein (RNP) complexes carry out this posttranscriptional processing. One component of RNA editing complexes is REAP-1, a protein of previously unknown function found primarily in mRNA containing editing complexes. We now show that REAP-1 is an RNA binding protein and map the binding activity to the amino-terminal third of the protein. REAP-1 binds to poly(G) and single-stranded guanosine rich RNAs. Data presented here demonstrates that preedited RNAs are the preferred substrate for REAP-1. The results suggest a model in which the role of REAP-1 is to bring preedited mRNAs into the editing complex.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Madison-Antenucci S,Hajduk SL

doi

10.1016/s1097-2765(01)00231-3

subject

Has Abstract

pub_date

2001-04-01 00:00:00

pages

879-86

issue

4

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(01)00231-3

journal_volume

7

pub_type

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