期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 114, 期 33, 页码 8883-8888出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1705815114
关键词
SLO2; DYW2; NUWA; PPR; RNA editing
资金
- Research Foundation Flanders [G.0C84.14N]
- Marie Curie long-term postdoctoral fellowship [FP7-PEOPLE-2009-IEF-252503]
- Netherlands Organization for Scientific Research (NWO) [VIDI-864.13.001]
- NWO (ERA-CAPS Project EURO-PEC) [849.13.006]
- Deutsche Forschungsgemeinschaft [TA624/4-2, TA624/-1, TA624/10-1]
Recent identification of several different types of RNA editing factors in plant organelles suggests complex RNA editosomes within which each factor has a different task. However, the precise protein interactions between the different editing factors are still poorly understood. In this paper, we show that the E+-type pentatricopeptide repeat (PPR) protein SLO2, which lacks a C-terminal cytidine deaminase-like DYW domain, interacts in vivo with the DYW-type PPR protein DYW2 and the P-type PPR protein NUWA in mitochondria, and that the latter enhances the interaction of the former ones. These results may reflect a protein scaffold or complex stabilization role of NUWA between E+-type PPR and DYW2 proteins. Interestingly, DYW2 and NUWA also interact in chloroplasts, and DYW2-GFP overexpressing lines show broad editing defects in both organelles, with predominant specificity for sites edited by E+-type PPR proteins. The latter suggests a coordinated regulation of organellar multiple site editing through DYW2, which probably provides the deaminase activity to E+ editosomes.
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