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Nucleic Acids Research, 1989, Vol. 17, No. 8 3145-3161
© 1989

MOLECULAR BIOLOGY

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

Robert C. Bruckner and Michael M. Cox*

Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin-Madison Madison, WI 53706. USA

*To whom correspondence should be addressed

Received December 21, 1988. Revised February 23, 1989. Accepted February 23, 1989.

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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