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Crystal structure of the chloroplast RNA editing factor MORF2

Journal Article · · Biochemical and Biophysical Research Communications
; ;  [1]
  1. School of Life Sciences, Anhui University, 111 Jiulong Road, Hefei, Anhui, 230601 (China)
Highlights: • Crystal structure of MORF2 is determined at 2.4 Å. • MORF2 forms dimer through hydrophobic interaction. • Dimerization interface of MORF2 overlaps with its PPR interacting site. • A dimer-to-monomer transition is implicated for MORF2's role in RNA editing. RNA editing is a post-transcription process that alters the genetic information on RNA molecules. In plastids and mitochondria of flowering plants, the multiple organellar RNA editing factors (MORFs) interact with the PLS-type pentatricopeptide repeat (PPR) proteins and participate in RNA editing of cytidine-to-uridine conversion. The PPR proteins recognize cytidine targets around the editing sites, and the MORF proteins modulate the RNA-binding activity of the PPR proteins. Here, we report the structure of the Arabidopsis thaliana chloroplast MORF2 at 2.4 Å resolution. The structure, adopting typical MORF-box fold as observed in mitochondrial MORF1 and chloroplast MORF9, reveals an MORF1-like dimerization mode. The difference between the two dimerization modes can be attributed to F157 (corresponding F162 in MORF1 and W160 in MORF9), which causes a 60° shift upon dimerization. This observation, together with the PPR–MORF2 model, suggests a dimer-to-monomer transition during RNA editosome formation.
OSTI ID:
23134378
Journal Information:
Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 2 Vol. 495; ISSN 0006-291X; ISSN BBRCA9
Country of Publication:
United States
Language:
English

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