title: Correlation of chloroplast and bacterial ribosomal proteins by cross-reactions of antibodies specific to purified Escherichia coli ribosomal proteins.
abstract: Immunological homology between chloroplast ribosomal proteins (r-proteins) from a higher plant (Spinacia) and bacterial r-proteins was examined using antibodies prepared against 35 purified Escherichia coli r-proteins. Cross-reactions were determined on cellulose acetate gels and on nitrocellulose paper, after electrophoretic transfer of r-proteins from one- and two dimensional polyacrylamide gels, using peroxidase and fluorescein-conjugated second antibodies for detection (immunoblotting). The specificity of positive cross-reactions was confirmed by absorption experiments using purified E. coli r-proteins. Antisera against five proteins of the small subunit and six proteins of the large subunit of E. coli ribosome (i.e. anti-S7, -S9, -S11, -S12, and -S19; anti-L1, -L2, -L3, -L6, -L13, and -L17) gave cross-reactions. As an inference from this work, and a recent study on the synthesis of certain chloroplast r-proteins in isolated chloroplasts (Eneas-Filho, J., Hartley, M. R., and Mache, R. (1981) Mol. Gen. Genet. 184, 484-488), we suggest that chloroplast r-proteins S7 and L2 are encoded in the organelle DNA.
authors.forename: M
authors.initials: M
authors.lastname: Bartsch
mesh_terms: D000906:Antibodies; D000936:Antigen-Antibody Complex; D002736:Chloroplasts / Q000032:analysis*; D003429:Cross Reactions; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes / Q000032:analysis; D004926:Escherichia coli / Q000032:analysis*; D007124:Immunoenzyme Techniques; D010944:Plants / Q000032:analysis*; D012269:Ribosomal Proteins / Q000032:analysis*; D012270:Ribosomes / Q000032:analysis
chemical_list: D000906:Antibodies; D000936:Antigen-Antibody Complex; D000939:Epitopes; D012269:Ribosomal Proteins