Purification of the Escherichia coli purine regulon repressor and identification of corepressors.

Abstract:

:The Escherichia coli pur regulon repressor protein was overproduced in a phage T7 expression system. The overexpressed repressor constituted approximately 35% of the soluble cellular protein. Pur repressor was purified to near homogeneity by two chromatographic steps. Hypoxanthine or guanine was required for binding of purified repressor to purF operator DNA. Apparent dissociation constants of 3.4 nM were determined for binding of holorepressor to purF operator and of 1.7 and 7.1 microM were determined for aporepressor interaction with guanine and hypoxanthine, respectively. A requirement for hypoxanthine or guanine for conversion of aporepressor to holorepressor in vitro supports the earlier report (U. Houlberg and K.F. Jensen, J. Bacteriol. 153:837-845, 1983) that these purine bases are involved in regulation of pur gene expression in Salmonella typhimurium and confirms that hypoxanthine and guanine are corepressors.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Rolfes RJ,Zalkin H

doi

10.1128/jb.172.10.5637-5642.1990

subject

Has Abstract

pub_date

1990-10-01 00:00:00

pages

5637-42

issue

10

eissn

0021-9193

issn

1098-5530

journal_volume

172

pub_type

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