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Mass Spectrometric Characterization of Sequence-Specific Complexes of DNA and Transcription Factor PU.1 DNA Binding Domain

Authors
Journal
Analytical Biochemistry
0003-2697
Publisher
Elsevier
Publication Date
Volume
239
Issue
1
Identifiers
DOI: 10.1006/abio.1996.0287
Disciplines
  • Biology

Abstract

Abstract Electrospray ionization mass spectrometry (ESI–MS) has been used to study the noncovalent interaction of the 13.5-kDa DNA binding domain of PU.1 (PU.1-DBD) with specific double-stranded DNA (dsDNA) target molecules. Mixtures of PU.1-DBD protein and wild-type target DNA sequence yielded ESI–MS spectra showing only protein–dsDNA complex ions of 1:1 stoichiometry and free dsDNA. When PU.1-DBD protein, wild type target DNA, and a mutant target DNA lacking the consensus sequence were mixed, only the 1:1 complex with the wild-type DNA was observed, consistent with gel electrophoresis mobility shift assay results, demonstrating the observation of sequence-specific protein–dsDNA complexes using ESI–MS.

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