Details

Autor(en) / Beteiligte

• Schultheiss, J
• Kunert, O
• Gase, U
• Scharf, K.D
• Nover, L
• Ruterjans, H

Titel

Solution structure of the DNA-binding domain of the tomato heat-stress transcription factor HSF24

Ist Teil von

• European journal of biochemistry, 1996-03, Vol.236 (3), p.911-921

Ort / Verlag

Oxford, UK: Blackwell Science Ltd

Erscheinungsjahr

1996

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• Two-dimensional-NMR and three-dimensional-NMR experiments were performed to determine the solution structure of the DNA-binding domain of the tomato heat-stress transcription factor HSF24. Samples of uniformly 15N-labeled and 15N, 13C-labeled recombinant proteins were used in the investigation. A near-complete assignment of the backbone 1H 15N, and 13C resonances was obtained by three-dimensional triple-resonance experiments, whereas three-dimensional 15N-TOCSY-heteronuclear-single-quantum -correlation-spectroscopy, HCCH-COSY and HCCH-TOCSY spectra were recorded for side-chain assignments. 885 non-redundant distance constraints from two-dimensional-homonuclear and three-dimensional-15N-edited and 13C-edited NOESY spectra and 40 hydrogen-bond constraints from exchange experiments were used for structure calculations. The resulting three-dimensional structure contains a three-helix bundle and a small four-stranded antiparallel beta-sheet that forms a hydrophobic core. The two C-terminal helices are parts of a highly conserved helix-turn-helix motif that is probably involved in DNA recognition and binding. In contrast to heat-stress factors from yeast and animals, the plant heat-stress factors lack a loop of 11 amino acid residues inserted between beta 3 and beta 4. This leads to a tight turn between these beta-strands.