Effects of DNA binding and metal substitution on the dynamics of the GAL4 DNA-binding domain as studied by amide proton exchange

T. Mau, J. D. Baleja, G. Wagner

Research output: Contribution to journalArticle

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Abstract

Backbone amide proton exchange rates in the DNA-binding domain of GAL4 have been determined using 1H-15N heteronuclear correlation NMR spectroscopy. Three forms of the protein were studied - the native Zn-containing protein, the Cd-substituted protein, and a Zn-GAL4/DNA complex. Exchange rates in the Zn-containing protein are significantly slower than in the Cd-substituted protein. This shows that Cd-substituted GAL4 is destabilized relative to the native Zn-containing protein. Upon DNA binding, global retardation of amide proton exchange with solvent was observed, indicating that internal fluctuations of the DNA-recognition module are significantly reduced by the presence of DNA. In all forms of the protein, the internal dyad symmetry of the DNA-recognition module of GAL4 is reflected by the backbone amide proton exchange rates.

Original languageEnglish (US)
Pages (from-to)1403-1412
Number of pages10
JournalProtein Science
Volume1
Issue number11
StatePublished - 1992

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Amides
Protons
Substitution reactions
Metals
DNA
Proteins
Biomolecular Nuclear Magnetic Resonance
Nuclear magnetic resonance spectroscopy
Magnetic Resonance Spectroscopy

ASJC Scopus subject areas

  • Biochemistry

Cite this

Effects of DNA binding and metal substitution on the dynamics of the GAL4 DNA-binding domain as studied by amide proton exchange. / Mau, T.; Baleja, J. D.; Wagner, G.

In: Protein Science, Vol. 1, No. 11, 1992, p. 1403-1412.

Research output: Contribution to journalArticle

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