Escherichia Coli OxyR Modulation of Bacteriophage Mu Mom Expression in Dam+ Cells Can Be Attributed to Its Ability to Bind Hemimethylated Pmom Promoter DNA

Overview

Journal Nucleic Acids Res

Publisher Oxford University Press

Specialty Biochemistry

Date 1997 Oct 23

PMID 9336472

Citations 10

Authors

S Hattman

W Sun

Affiliations

Soon will be listed here.

Abstract

Transcription of the bacteriophage Mu mom operon is strongly repressed by the host OxyR protein in dam - but not dam + cells. In this work we show that the extent of mom modification is sensitive to the relative levels of the Dam and OxyR proteins and OxyR appears to modulate the level of mom expression even in dam + cells. In vitro studies demonstrated that OxyR is capable of binding hemimethylated P mom , although its affinity is reduced slightly compared with unmethylated DNA. Thus, OxyR modulation of mom expression in dam + cells can be attributed to its ability to bind hemimethylated P mom DNA, the product of DNA replication.

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