The histone-like H protein of Escherichia coli is ribosomal protein S3.

AUTOR(ES)

Bruckner, R C

RESUMO

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.

Documentos Relacionados

• Role of Histone-Like Protein H-NS in Multidrug Resistance of Escherichia coli
• Histone-like proteins in the purified Escherichia coli deoxyribonucleoprotein
• Regulation of lysyl-tRNA synthetase expression by histone-like protein H-NS of Escherichia coli.
• Anucleate cell production by Escherichia coli delta hns mutant lacking a histone-like protein, H-NS.
• Alterations of the outer membrane composition in Escherichia coli lacking the histone-like protein HU