PMID:2657655
| Citation |
Bruckner, RC and Cox, MM (1989) The histone-like H protein of Escherichia coli is ribosomal protein S3. Nucleic Acids Res. 17:3145-61 |
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| Abstract |
We report the purification of four proteins from Escherichia coli that stimulate or inhibit inter- and/or intramolecular recombination promoted by the yeast plasmid-encoded FLP protein. The proteins are identified as the ribosomal proteins S3 (27 kDa), L2 (26 kDa), S4 (24 kDa), and S5 (16 kDa), on the basis of N-terminal sequence analysis. The S3 protein is found to be identical to H protein, an E. coli histone-like protein that is related to histone H2A immunologically and by virtue of amino acid content. The H protein/S3 identity is based on co-migration on polyacrylamide gels, heat stability, amino acid analysis, and effects on FLP-promoted recombination. These results are relevant to current studies on the structure of the E. coli nucleoid. Since the H protein has previously been found associated with the E. coli nucleoid, the results indicate that either (a) some ribosomal proteins serve a dual function in E. coli, or, more likely, (b) ribosomal proteins can and are being mis-identified as nucleoid constituents. |
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| Keywords |
Amino Acid Sequence; Bacterial Proteins/physiology; Chromosomes, Bacterial/ultrastructure; DNA, Bacterial/metabolism; DNA-Binding Proteins/isolation & purification; DNA-Binding Proteins/physiology; Escherichia coli/physiology; Histones/physiology; Molecular Sequence Data; Recombination, Genetic; Ribosomal Proteins/isolation & purification; Ribosomal Proteins/physiology; Saccharomyces cerevisiae/genetics |
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