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Review |
appropriation: remodelling of the
70 subunit of Escherichia coli RNA polymerase by the bacteriophage T4 activator MotA and co-activator AsiA



Laboratory of Molecular and Cellular Biology, National Institute of Diabetes Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA
Correspondence
Deborah M. Hinton
dhinton{at}helix.nih.gov
Activation of bacteriophage T4 middle promoters, which occurs about 1 min after infection, uses two phage-encoded factors that change the promoter specificity of the host RNA polymerase. These phage factors, the MotA activator and the AsiA co-activator, interact with the
70 specificity subunit of Escherichia coli RNA polymerase, which normally contacts the 10 and 35 regions of host promoter DNA. Like host promoters, T4 middle promoters have a good match to the canonical
70 DNA element located in the 10 region. However, instead of the
70 DNA recognition element in the promoter's 35 region, they have a 9 bp sequence (a MotA box) centred at 30, which is bound by MotA. Recent work has begun to provide information about the MotA/AsiA system at a detailed molecular level. Accumulated evidence suggests that the presence of MotA and AsiA reconfigures proteinDNA contacts in the upstream promoter sequences, without significantly affecting the contacts of
70 with the 10 region. This type of activation, which is called
appropriation, is fundamentally different from other well-characterized models of prokaryotic activation in which an activator frequently serves to force
70 to contact a less than ideal 35 DNA element. This review summarizes the interactions of AsiA and MotA with
70, and discusses how these interactions accomplish the switch to T4 middle promoters by inhibiting the typical contacts of the C-terminal region of
70, region 4, with the host 35 DNA element and with other subunits of polymerase.
Present address: National Oceanic and Atmospheric Administration, Silver Spring, MD, USA.
Present address: Center for Advanced Research in Biotechnology, University of Maryland, Rockville, MD, USA.
Present address: Trinity University, Washington, DC, USA.
||Present address: Institute of Systems Biology, Seattle, WA, USA.
¶Present address: Uniformed Services University of the Health Sciences, Bethesda, MD, USA.
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