Journal Article

Mutagenesis Analysis of the Interaction between the Dorsal Rel Homology Domain and HMG Boxes of DSP1 Protein

Davy Martin, Anne Daulny, Martine Decoville and Daniel Locker

in The Journal of Biochemistry

Published on behalf of The Japanese Biochemical Society

Volume 134, issue 4, pages 583-589
Published in print October 2003 | ISSN: 0021-924X
Published online October 2003 | e-ISSN: 1756-2651 | DOI:

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DSP1 is an HMG-like protein of Drosophila melanogaster consisting of 386 amino acids with two HMG domains at the C-terminal end. It was shown to interact with Dorsal protein through the HMG domains and to enhance its DNA binding. Each HMG domain consists of approximately 80 amino acid residues, forming three alpha helices folded into an L-shaped structure. We have compared the interaction of various truncated and mutated forms of DSP1 with the dorsal Rel homology domain (RHD). In particular, we have mutated the conserved tryptophan residue 212 or 302 in A or B boxes or the lysine-rich region (253KKRK256) of the A/B linker. Analysis by circular dichroism revealed that the protein tertiary structure is affected in these mutants. However, these mutations do not abolish the DSP1 binding to Dorsal, except if the two HMG boxes are altered, i.e., in a double mutant or in mutant isolated domain. Finally, studies on the enhancement of Dorsal DNA binding by DSP1 revealed that the DNA affinity is maximum in the presence of wild-type DSP1, is dramatically reduced when box A is altered, and is completely abolished when box B is altered.

Keywords: Key words: Dorsal, Drosophila, DSP1, HMGB, protein–protein interaction.

Journal Article.  4735 words.  Illustrated.

Subjects: Biochemistry