Higher plants utilize protein complexes to precisely edit hundreds of RNA transcripts in organelles. The mechanistic model of RNA editing involves a C‐to‐U deamination reaction facilitated through the interaction of the RNA with a protein complex. Complex models have been proposed, but the minimal “editosome” capable of catalyzing C‐to‐U changes and the functions of many of the protein components have not been revealed. This research focuses on describing the functional role of one critical protein component belonging to the RAN binding protein 2 type zinc fingers protein family, Organelle Zinc finger 1 (OZ1). Zinc finger proteins have been associated with RNA binding; though RNA binding and site recognition in editosomes is known to occur via PPR proteins, OZ1 may be interacting with a scaffold RNA sequence. Recombinant OZ1 from Arabidopsis thaliana was used to analyze zinc coordination and RNA binding of this zinc finger protein. Spectrophotometric analysis of OZ1 after immobilized metal affinity chromatography (IMAC) suggests nucleic acid association. ICP‐MS and ESI‐MS analysis of a truncated variant of OZ1, only the sequence containing its two zinc finger domains (OZ1zf), suggests that OZ1 is coordinating only one zinc ion instead of the proposed two. Computational analysis of OZ1 dependent sites in Brachypodium distachyon returned a potential motif conserved among OZ1‐dependent editing sites. Electrophoretic mobility shift assays (EMSAs) are used to test RNA binding and the motif. Understanding this protein will bring us a step closer to manipulating this precise editing machine for use in biotechnology and may be used for purposes of crop improvement.Support or Funding InformationFunding for this work was provided by NIH SCORE SC2 ID: SC2 GM122718 awarded to Dr. Michael L. Hayes and the NIH MBRS‐RISE R25 GM 061331‐17 grant in support of Alfredo Jimenez‐Salinas.