Quantitation with monoclonal antibodies of Escherichia coli H protein suggests histone function
Author(s) -
H. Lutz,
K. von Meyenburg,
Ulrich Hübscher
Publication year - 1985
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.162.3.1005-1007.1985
Subject(s) - biology , escherichia coli , microbiology and biotechnology , monoclonal antibody , histone , protein a/g , protein g , antibody , biochemistry , dna , genetics , recombinant dna , gene , fusion protein
The abundance of the histonelike H protein of Escherichia coli (U. Hübscher, H. Lutz, and A. Kornberg, Proc. Natl. Acad. Sci. U.S.A. 77:5097-5101, 1980) was determined by using monoclonal antibodies against H protein, immunoblotting, and homogeneous H protein as a standard. H protein was found to be present at approximately 120,000 monomeric molecules per fast-growing E. coli cell. This amount of H protein corresponds to a ratio of one H protein molecule to approximately 200 base pairs of the bacterial chromosome. Together with previous results, these findings suggest that H protein has histonelike function similar to that of histone protein H2A, its counterpart in the eucaryotic cell.
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