A chloroplastic RNA‐binding protein is a new member of the PPR family

FEBS Letters

Delseny, Michel¹  Filipowicz, Witold²  Barnèche, Fredy¹  Echeverria, Manuel¹  Lahmy, Sylvie¹  Derancourt, Jean³ 

[1] Laboratoire ‘Génome et Développement des Plantes’, Université de Perpignan, UMR CNRS 5096 Avenue de Villeneuve, 66860 Perpignan Cedex, France;Friedrich Miescher-Institut, P.O. Box 2543, CH-4002 Basel, Switzerland;Centre de Recherches de Biochimie Macromoléculaire UPR1086 route de Mende, 34293 Montpellier Cedex 5, France

关键词: RNA-binding activity;    PPR motif;    Plant;    Chloroplast;    HA-tagging;    PPR motif;    pentatricopeptide motif;    RRM;    RNA recognition motif;    rRNA;    ribosomal RNA;    EMSA;    electrophoretic mobility shift assay;    aa;    amino acid;    bZIP;    basic leucine zipper;   

DOI  :  10.1016/S0014-5793(00)01935-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

P67, a new protein binding to a specific RNA probe, was purified from radish seedlings [Echeverria, M. and Lahmy, S. (1995) Nucleic Acids Res. 23, 4963–4970]. Amino acid sequence information obtained from P67 microsequencing allowed the isolation of genes encoding P67 in radish and Arabidopsis thaliana. Immunolocalisation experiments in transfected protoplasts demonstrated that this protein is addressed to the chloroplast. The RNA-binding activity of recombinant P67 was found to be similar to that of the native protein. A significant similarity with the maize protein CRP1 [Fisk, D.G., Walker, M.B. and Barkan, A. (1999) EMBO J. 18, 2621–2630] suggests that P67 belongs to the PPR family and could be involved in chloroplast RNA processing.

【 授权许可】

Unknown