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

FEBS Lett. 2000 Sep 1;480(2-3):255-60. doi: 10.1016/s0014-5793(00)01935-9.

Abstract

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 Airabidopsis 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Arabidopsis
  • Base Sequence
  • Brassica
  • Chloroplasts / metabolism*
  • Cloning, Molecular
  • DNA, Plant
  • Gene Expression
  • Genes, Plant
  • Molecular Sequence Data
  • Plant Proteins / classification
  • Plant Proteins / genetics
  • Plant Proteins / metabolism*
  • RNA, Messenger
  • RNA-Binding Proteins / classification
  • RNA-Binding Proteins / genetics
  • RNA-Binding Proteins / metabolism*
  • Recombinant Fusion Proteins / classification
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Subcellular Fractions

Substances

  • DNA, Plant
  • Plant Proteins
  • RNA, Messenger
  • RNA-Binding Proteins
  • Recombinant Fusion Proteins
  • p67 protein, Raphanus sativus