Identification of a plastid-specific ribosomal protein in the 30 S subunit of chloroplast ribosomes and isolation of the cDNA clone encoding its cytoplasmic precursor

We describe the isolation and characterization of a chloroplast ribosomal protein and a clone of its cDNA. This protein has no homology to any Escherichia coli ribosomal protein or to any known proteins. Due to this novel finding we propose it be called PSrp-1, i.e. a plastid-specific ribosomal prot...

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Bibliographic Details
Published in:The Journal of biological chemistry 1990-08, Vol.265 (22), p.12790-12795
Main Authors: Johnson, G.H. (Max-Planck-Institute fur Molekulare Genetik, Berlin, Federal Republic of Germany), Kruft, V, Subramanian, A.R
Format: Article
Language:English
Subjects:
ADN
Amino Acid Sequence
AMINO ACID SEQUENCES
CHLOROPLASTE
CHLOROPLASTS
Chloroplasts - metabolism
CLONACION
CLONAGE
CLONING
Cloning, Molecular
CLOROPLASTO
DNA
DNA - genetics
embl/jo5555
genbank/jo5555
Gene Library
genes
GENETICA
GENETICS
GENETIQUE
Molecular Sequence Data
Molecular Weight
Peptide Fragments - isolation & purification
Peptide Mapping
PLANT PROTEINS
Plants - genetics
Plants - metabolism
PROTEINAS VEGETALES
PROTEINE VEGETALE
PSrp-1 protein
Restriction Mapping
Ribosomal Proteins - isolation & purification
Ribosomal Proteins - metabolism
RIBOSOMAS
RIBOSOME
RIBOSOMES
Ribosomes - metabolism
Spinacea oleracea
SPINACIA OLERACEA
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Summary:We describe the isolation and characterization of a chloroplast ribosomal protein and a clone of its cDNA. This protein has no homology to any Escherichia coli ribosomal protein or to any known proteins. Due to this novel finding we propose it be called PSrp-1, i.e. a plastid-specific ribosomal protein. The precursor form of PSrp-1, deduced from the cDNA sequence, is 302-amino acid residues long. The mature PSrp-1, identified by amino-terminal sequencing, is a protein of 236 residues. The NH2-terminal 66 amino acids form the transit peptide that targets PSrp-1 into the chloroplast. We show that PSrp-1 is a protein of the chloroplast 30 S ribosomal subunit by Western blotting and sequencing the excised protein after two-dimensional gel electrophoresis. The possible evolutionary origin of PSrp-1 from the nucleated host cell of the endosymbiont theory is discussed.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)38228-6