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

• Published in: FEBS letters 2000-09, Vol.480 (2), p.255-260
• Main Authors: Lahmy, Sylvie, Barnèche, Fredy, Derancourt, Jean, Filipowicz, Witold, Delseny, Michel, Echeverria, Manuel
• Format: Article
• Language: English
• Subjects: aa, amino acid; Amino Acid Motifs; Amino Acid Sequence; Arabidopsis; Base Sequence; Brassica; bZIP, basic leucine zipper; Chloroplast; Chloroplasts - metabolism; Cloning, Molecular; DNA, Plant; EMSA, electrophoretic mobility shift assay; Gene Expression; Genes, Plant; HA-tagging; Molecular Sequence Data; Plant; Plant Proteins - classification; Plant Proteins - genetics; Plant Proteins - metabolism; PPR motif; PPR motif, pentatricopeptide motif; Recombinant Fusion Proteins - classification; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - metabolism; RNA, Messenger; RNA-binding activity; RNA-Binding Proteins - classification; RNA-Binding Proteins - genetics; RNA-Binding Proteins - metabolism; RRM, RNA recognition motif; rRNA, ribosomal RNA; Subcellular Fractions
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(00)01935-9

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.