The CBS domain protein MJ0729 of Methanocaldococcus jannaschii binds DNA

被引:16
作者
Aguado-Llera, David [2 ]
Oyenarte, Iker [1 ]
Alfonso Martinez-Cruz, Luis [1 ]
Neira, Jose L. [2 ,3 ]
机构
[1] CIC bioGUNE, Unidad Biol Estruct, Derio 48160, Vizcaya, Spain
[2] Univ Miguel Hernandez, Inst Biol Mol & Celular, Elche 03202, Alicante, Spain
[3] Inst Biocomputac & Fis Sistemas Complejos, Zaragoza 50009, Spain
关键词
DNA; CBS domain; Fluorescence; Circular dichroism; NMR; Binding; SEQUENCE; REGION; FORM;
D O I
10.1016/j.febslet.2010.10.006
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
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 similar to 10 mu M. These results suggest that CBS domains might interact with DNA. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:4485 / 4489
页数:5
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