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 Celljournal_title
Molecular cellauthors
Madison-Antenucci S,Hajduk SLdoi
10.1016/s1097-2765(01)00231-3subject
Has Abstractpub_date
2001-04-01 00:00:00pages
879-86issue
4eissn
1097-2765issn
1097-4164pii
S1097-2765(01)00231-3journal_volume
7pub_type
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