The MotA transcriptional activator of bacteriophage T4 binds to its specific DNA site as a monomer

Biochemistry
M P CiceroK N Kreuzer

Abstract

During bacteriophage T4 middle mode gene expression, the MotA transcription factor binds to T4 middle promoters at a -30 mot box consensus sequence to allow activation. Previous binding studies showed that MotA forms multiple gel-shifted complexes with DNA, and structural evidence suggested that MotA dimerizes upon DNA binding. We have shown that a short (13 bp) mot box DNA substrate binds MotA protein but fails to form slower migrating complexes. Therefore, the slower migrating complexes in gel shift assays are caused by DNA-mediated binding events. Competition experiments indicate that the slower migrating complexes are formed by nonspecific binding events, while the first-shifted complex is caused by specific binding to the mot box. Saturation binding experiments revealed that the stoichiometry of MotA binding to DNA is 1:1 in the first-shifted complex, while the slower complexes apparently contain MotA multimers. Gel shift assays using mixtures of MotA and a GST-MotA fusion protein supported the conclusion that the first-shifted complex contains one protein molecule bound to DNA. Furthermore, MotA monomers were cross-linked by glutaraldehyde under conditions where slower complexes exist, but not under conditions that lead t...Continue Reading

References

Nov 5, 1992·Nature·D B NikolovS K Burley
Nov 15, 1996·Journal of Molecular Biology·E SeverinovaS A Darst
Apr 15, 1997·The EMBO Journal·M S FinninK N Kreuzer

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Citations

Mar 11, 2003·Microbiology and Molecular Biology Reviews : MMBR·Eric S MillerWolfgang Rüger
Oct 30, 2010·Virology Journal·Deborah M Hinton
Sep 28, 2005·Journal of Molecular Biology·Brian D GregoryAnn Hochschild
Aug 2, 2013·The Journal of Biological Chemistry·Meng-Lun HsiehDeborah M Hinton
Mar 21, 2002·Journal of Molecular Biology·Lidija TruncaiteRimas Nivinskas

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