z-logo
open-access-imgOpen Access
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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom