Metal ion co-ordination in the DNA binding domain of the yeast transcriptional activator GAL4

The structure of the DNA binding domain of the yeast transcriptional activator GAL4 was investigated by extended X-ray fine structure (e.x.a.f.s.). Two samples of GAL4 were studied, one containing cadmium as a structural probe (Cd(II)GAL4) and the other containing the ‘native’ zinc (Zn(Il)-GAL4). Th...

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Veröffentlicht in:	FEBS letters 1990-06, Vol.266 (1), p.142-146
Hauptverfasser:	Povey, Jane F., Diakun, Gregory P., Garner, C.David, Wilson, Stephen P., Laue, Ernest D.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Binding and carrier proteins Biological and medical sciences Cadmium Cations, Divalent DNA DNA binding DNA-Binding Proteins - metabolism DNA-Binding Proteins - ultrastructure Extended X-ray fine structure Fourier Analysis Fundamental and applied biological sciences. Psychology Fungal Proteins - metabolism Fungal Proteins - ultrastructure GAL4 GAL4 protein In Vitro Techniques Proteins Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Spectrum Analysis Structure Sulfur Transcription Factors - metabolism Transcription Factors - ultrastructure X-ray diffraction X-Rays Zinc Zinc finger
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Zusammenfassung:	The structure of the DNA binding domain of the yeast transcriptional activator GAL4 was investigated by extended X-ray fine structure (e.x.a.f.s.). Two samples of GAL4 were studied, one containing cadmium as a structural probe (Cd(II)GAL4) and the other containing the ‘native’ zinc (Zn(Il)-GAL4). The results suggest that the structure of the DNA binding domain of GAL4 contains a two metal ion cluster distinguishing it from the ‘zinc finger’ proteins typified by the Xenopus laevis transcription factor TFIIIA.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(90)81525-S