2026-04-17T07:00:26Zhttps://recercat.cat/oai/request

oai:recercat.cat:2117/781172026-01-18T05:04:45Zcom_2072_1033col_2072_452950

00925njm 22002777a 4500 dc Sánchez Giraldo, Raquel author Acosta Reyes, Francisco Javier author Malarkey, Christopher S. author Saperas Plana, Núria author Churchill, Mair E. A. author Campos López, Josefina de Lourdes author 2015-07-02 High-mobility group protein 1 (HMGB1) is an essential and ubiquitous DNA architectural factor that influences a myriad of cellular processes. HMGB1 contains two DNA-binding domains, box A and box B, which have little sequence specificity but have remarkable abilities to underwind and bend DNA. Although HMGB1 box A is thought to be responsible for the majority of HMGB1-DNA interactions with pre-bent or kinked DNA, little is known about how it recognizes unmodified DNA. Here, the crystal structure of HMGB1 box A bound to an AT-rich DNA fragment is reported at a resolution of 2 angstrom. Two box A domains of HMGB1 collaborate in an unusual configuration in which the Phe37 residues of both domains stack together and intercalate the same CG base pair, generating highly kinked DNA. This represents a novel mode of DNA recognition for HMGB proteins and reveals a mechanism by which structure-specific HMG boxes kink linear DNA. Peer Reviewed Postprint (published version) Àrees temàtiques de la UPC::Enginyeria química DNA-protein interactions High-mobility group protein X-ray crystallography DNA binding hmgb1 cisplatin-modified dna mitochondrial transcription factor 4-way junction dna tandem hmg boxes intercalating residues binding proteins histone h1 duplex dna a-domain chromatin ADN -- Interaccions de les proteïnes Two high-mobility group box domains act together to underwind and kink DNA.