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 Microbioljournal_title
Molecular microbiologyauthors
Webster C,Merryweather A,Brammar Wdoi
10.1111/j.1365-2958.1992.tb01480.xsubject
Has Abstractpub_date
1992-02-01 00:00:00pages
371-7issue
3eissn
0950-382Xissn
1365-2958journal_volume
6pub_type
杂志文章abstract::Two-component signal transduction (TCST) pathways are regulatory systems that are highly homologous throughout the bacterial kingdom. Their established role in virulence and absence in vertebrates has made TCST an attractive target for therapeutic intervention. However, such systems have yet to yield success in the de...
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pub_type: 杂志文章
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更新日期:2003-09-01 00:00:00
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更新日期:2005-04-01 00:00:00
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journal_title:Molecular microbiology
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更新日期:2002-01-01 00:00:00
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pub_type: 评论,杂志文章
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