Antibodies directed against E. coli ribosomal protein S1 were used in immunoblotting assays to search for an S1-like protein in the ribosome of spinach chloroplast. An immunological cross-reaction was reproducibly detected on the blots and inhibition experiments have demonstrated its specificity. Th
Comparison of ribosomal proteins of chloroplast from Spinach and of E. coli
β Scribed by Dorne, A. M. ;Eneas-Filho, J. ;Heizmann, P. ;Mache, R.
- Publisher
- Springer
- Year
- 1984
- Tongue
- English
- Weight
- 632 KB
- Volume
- 193
- Category
- Article
- ISSN
- 0026-8925
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β¦ Synopsis
A comparison of ribosomal proteins from Escherichia coli and from chloroplasts of Spinach was made using two separate methods: electrophoretic migration and immunochemical cross-reaction between blotted E. coli ribosomal proteins and chloroplast ribosomal subunits antisera. It is shown that L2 from E. coli (E-L2) and L4 from chloroplasts (CS-L4) comigrated and that E-L2 immunologically cross-reacted with the isolated CS-L4 antibody. Co-migration was observed for three additional couples of 50S ribosomal proteins. It is also shown that at least one 30S E. coli ribosomal protein immuno-cross reacted with a 30S chloroplast antiserum and that three couples of 30S ribosomal proteins comigrated.
π SIMILAR VOLUMES
A full size cDNA clone encoding the chloroplast ribosomal protein L21 from spinach is presented. The identity of the clone and the location of the transit peptide processing site were determined by comparison with the N-terminal amino acid sequence of the spinach chloroplast protein CS-L7 previously
The map location and nucleotide sequence of the genes for the $4 ribosomal protein (rps4) and for tRNA xhr (UGU) (trnT) and tRNA ser (GGA) (trnS) on spinach chloroplast DNA have been determined, rps4 lies approximately 5 kb 3' to atpBE in the large single copy region and is transcribed in the same d