Kinetoplastid RNA-editing-associated protein 1 (REAP-1): a novel editing complex protein with repetitive domains

• Published in: The EMBO journal Vol. 17; no. 21; pp. 6368 - 6376
• Main Authors: Madison-Antenucci, Susan, Sabatini, Robert S., Pollard, Victoria W., Hajduk, Stephen L.
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 02.11.1998
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Cloning, Molecular; Fluorescent Antibody Technique; kinetoplastid RNA; Microscopy, Fluorescence; Molecular Sequence Data; Protozoan Proteins - chemistry; Protozoan Proteins - genetics; REAP-1; Recombinant Proteins - genetics; ribonucleoprotein (RNP) complex; Ribonucleoproteins - chemistry; Ribonucleoproteins - genetics; RNA - genetics; RNA editing; RNA Editing - genetics; RNA Ligase (ATP) - genetics; RNA Nucleotidyltransferases - genetics; Sequence Analysis, DNA; Trypanosoma brucei brucei - genetics
• ISSN: 0261-4189; 1460-2075
• DOI: 10.1093/emboj/17.21.6368

Kinetoplastid RNA editing consists of the addition or deletion of uridines at specific sites within mitochondrial mRNAs. This unusual RNA processing event is catalyzed by a ribonucleoprotein (RNP) complex that includes editing site‐specific endoribonuclease, RNA ligase and terminal uridylnucleotidyl transferase (Tutase) among its essential enzymatic activities. To identify the components of this RNP, monoclonal antibodies were raised against partially purified editing complexes. One antibody reacts with a mitochondrially located 45 kDa polypeptide (p45) which contains a conserved repetitive amino acid domain. p45 co‐purifies with RNA ligase and Tutase in a large (∼700 kDa) RNP, and anti‐p45 antibody inhibits in vitro RNA editing. Thus, p45 is the first kinetoplastid RNA‐editing‐associated protein (REAP‐1) that has been cloned and identified as a protein component of a functional editing complex.