Premium
The CBS domain protein MJ0729 of Methanocaldococcus jannaschii binds DNA
Author(s) -
Aguado-Llera David,
Oyenarte Iker,
Martínez-Cruz Luis Alfonso,
Neira José L.
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.10.006
Subject(s) - dna , biology , dna binding domain , dna binding protein , biochemistry , transcription (linguistics) , hmg box , transcription factor , gene , genetics , microbiology and biotechnology , linguistics , philosophy
The cystathionine beta‐synthase (CBS) domains function as regulatory motifs in several proteins. Elucidating how CBS domains exactly work is relevant because several genetic human diseases have been associated with mutations in those motifs. Here, we show, for the first time, that a CBS domain binds calf‐thymus DNA and E‐boxes recognized by transcription factors. We have carried out the DNA‐binding characterization of the CBS domain protein MJ0729 from Methanocaldococcus jannaschii by biochemical and spectroscopic techniques. Binding induces conformational changes in the protein, and involves the sole tryptophan residue. The apparent dissociation constant for the E‐boxes is ∼10 μM. These results suggest that CBS domains might interact with DNA.