Efficient repression by a heterodimeric repressor in Escherichia coli.

Abstract:

:Previous studies with purified variants of the 434 repressor having different operator-binding specificities have demonstrated the interactions of a heterodimeric repressor with a hybrid operator site. The present study investigates the interactions between the 434 repressor and its operator site. The optimum 434 operator half-site is used with a P22 operator half-site to create a hybrid 434/P22 operator. We show that this hybrid operator can be efficiently bound by a heterodimeric repressor, consisting of one wild-type 434 repressor monomer and one 434 repressor monomer with the binding specificity of the P22 repressor, to bring about repression in Escherichia coli.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Webster C,Merryweather A,Brammar W

doi

10.1111/j.1365-2958.1992.tb01480.x

subject

Has Abstract

pub_date

1992-02-01 00:00:00

pages

371-7

issue

3

eissn

0950-382X

issn

1365-2958

journal_volume

6

pub_type

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