SRY, like HMG1, recognizes sharp angles in DNA

• Published in: The EMBO journal 1992-12, Vol.11 (12), p.4497-4506
• Main Authors: Ferrari, S., Harley, V.R., Pontiggia, A., Goodfellow, P.N., Lovell‐Badge, R., Bianchi, M.E.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Biological and medical sciences; DNA - chemistry; DNA - metabolism; DNA-Binding Proteins - metabolism; Electrophoresis, Polyacrylamide Gel; Fundamental and applied biological sciences. Psychology; High Mobility Group Proteins - metabolism; Humans; Interactions. Associations; Intermolecular phenomena; Molecular biophysics; Molecular Sequence Data; Nuclear Proteins; Nucleic Acid Conformation; Plasmids; Protein Binding; Sequence Homology, Amino Acid; Sex-Determining Region Y Protein; Substrate Specificity; Transcription Factors
• ISSN: 0261-4189; 1460-2075
• DOI: 10.1002/j.1460-2075.1992.tb05551.x

HMG boxes are DNA binding domains present in chromatin proteins, general transcription factors for nucleolar and mitochondrial RNA polymerases, and gene‐ and tissue‐specific transcriptional regulators. The HMG boxes of HMG1, an abundant component of chromatin, interact specifically with four‐way junctions, DNA structures that are cross‐shaped and contain angles of approximately 60 and 120 degrees between their arms. We show here also that the HMG box of SRY, the protein that determines the expression of male‐specific genes in humans, recognizes four‐way junction DNAs irrespective of their sequence. In addition, when SRY binds to linear duplex DNA containing its specific target AACAAAG, it produces a sharp bend. Therefore, the interaction between HMG boxes and DNA appears to be predominantly structure‐specific. The production of the recognition of a kink in DNA can serve several distinct functions, such as the repair of DNA lesions, the folding of DNA segments with bound transcriptional factors into productive complexes or the wrapping of DNA in chromatin.