Determination of protein‐only RNase P interactome in Arabidopsis mitochondria and chloroplasts identifies a complex between PRORP1 and another NYN domain nuclease
Author:
Affiliation:
1. Institut de biologie moléculaire des plantes CNRS Université de Strasbourg Strasbourg France
2. Plateforme protéomique Strasbourg‐Esplanade CNRS Université de Strasbourg 15 rue René Descartes Strasbourg F‐67084 France
Funder
Centre National de la Recherche Scientifique
Université de Strasbourg
Agence Nationale de la Recherche
Publisher
Wiley
Subject
Cell Biology,Plant Science,Genetics
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1111/tpj.14458
Reference59 articles.
1. A view of RNase P
2. The NYN Domains: Novel Predicted RNAses with a PIN Domain-Like Fold
3. OST-HTH: a novel predicted RNA-binding domain
4. The Mitochondrial RNA-Binding Protein GRSF1 Localizes to RNA Granules and Is Required for Posttranscriptional Mitochondrial Gene Expression
5. Structural Basis for the Versatile Interactions of Smad7 with Regulator WW Domains in TGF-β Pathways
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2. The protein‐only RNase Ps, endonucleases that cleave pre‐tRNA: Biological relevance, molecular architectures, substrate recognition and specificity, and protein interactomes;WIREs RNA;2024-03
3. Discovery, structure, mechanisms, and evolution of protein-only RNase P enzymes;Journal of Biological Chemistry;2024-03
4. A tRNA-modifying enzyme facilitates RNase P activity in Arabidopsis nuclei;Nature Plants;2023-11-09
5. A unique C‐terminal domain contributes to the molecular function of Restorer‐of‐fertility proteins in plant mitochondria;New Phytologist;2023-08-07
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