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Preliminary investigation of the interaction between the R2R3 DNA binding domain of the oncoprotein c-Myb and DNA fragments

✍ Scribed by Nadège Jamin; Véronique Le Tilly; Loussinee Zargarian; Anne Bostad; Iris Besançon-Yoshpe; Pierre-Noël Lirsac; Odd S. Gabrielsen; Flavio Toma

Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
612 KB
Volume
59
Category
Article
ISSN
0020-7608

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✦ Synopsis

The interaction between the R2R3 DNA binding domain of the oncoprotein c-Myb and oligodeoxynucleotides was investigated by ' H-NMR spectroscopy and fluorescence anisotropy assays. Titration of 12 and 16 base-pair DNA fragments containing the TAACGGTC sequence with R2R3 revealed the presence of two complexed forms (in a 40/60 ratio) either two complexes or two conformations in slow exchange at the NMR chemical shift time scale. The largest variations of imino proton chemical shifts were observed for the imino proton of the base pairs 2, 3, 4 and 6 of the DNA sequence, suggesting a direct involvement of these base pairs in the interaction. Using fluorescence anisotropy measurements, a dissociation constant of 5.12 k 1.49 n M for the specific DNA-R2R3 complex was found, whereas a value of 2.7 f 0.1 p M was determined for the nonspecific complex.

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