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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
MeSH Review

HMG-Box Domains

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High impact information on HMG-Box Domains

  • SRY encodes a protein with a central 'high mobility group' domain (HMG box) of about 78 amino acids [1].
  • We show that HMG1 interacts with proteins encoded by the HOX gene family by establishing protein-protein contacts between the HMG box domains and the HOX homeodomain [2].
  • The bending activity was maintained by a 79-amino acid polypeptide corresponding to a single HMG-box domain of HMG1 [3].
  • The CP components Cdc68 and Pob3 closely resemble the FACT components, except that the C-terminal high-mobility group (HMG) box domain of SSRP1 is not found in the yeast homolog Pob3 [4].
  • Mediated by its C-terminal high mobility group (HMG) box domain, SSRP1 binds DNA non-sequence specifically but recognizes certain DNA structures [5].

Biological context of HMG-Box Domains


Associations of HMG-Box Domains with chemical compounds

  • RESULTS: Pauciarticular, but not polyarticular, JRA patient sera were found to recognize a lysine-rich major epitope (KKGKKKDP), which is located in the linker region of the HMG box domains of the HMG-2 nonhistone chromosomal protein [9].
  • This interaction is mediated through a specific proline-rich domain in the N-terminal region of Alx4 and requires the DNA-binding domain (HMG-box) of LEF-1 [10].
  • Site-directed mutagenesis of intercalating residues in both HMG domains A and B in full-length HMGB1 further supports the conclusion that only one HMG box domain is bound to the site of cisplatin damage [11].
  • To examine whether the negative effect of the acidic C-terminal domain is brought about by interactions with the basic part of HMGB1 (N-terminal region, HMG-box domain), intramolecular cross-linking in combination with formic acid cleavage of the protein was used [12].
  • Mutational analysis of the HMG1 B-domain revealed that replacement of Lys96 of the extended N-terminal segment (and much less the neighboring Arg97) and Lys128 of helix II to glutamic acid severely impaired binding of the HMG box domain to supercoiled DNA [13].

Gene context of HMG-Box Domains

  • Both HMG box domains of HMGB1, A and B, interact with p73alpha [14].
  • Whereas L-Sox5 and Sox6 are highly homologous proteins, they are totally different from Sox9 outside the HMG box domain [15].
  • The HMG-box domain of the human male sex-determining factor SRY, hSRY(HMG) (comprising residues 57-140 of the full-length sequence), binds DNA sequence-specifically in the minor groove, resulting in substantial DNA bending [16].
  • To understand better the basis of this preference, we have studied the binding of HMG1 (which has two tandem HMG boxes linked by a basic extension to a long acidic tail) and Drosophila HMG-D (one HMG box linked by a basic region to a short and less acidic tail), and their HMG-box domains, to 88 bp and 75 bp DNA minicircles [17].
  • Among the six HMG box domains in hUBF, the first one can bind to the ribosomal promoter specifically by itself and is essential for the whole protein's DNA binding specificity [18].

Analytical, diagnostic and therapeutic context of HMG-Box Domains


  1. Rapid sequence evolution of the mammalian sex-determining gene SRY. Whitfield, L.S., Lovell-Badge, R., Goodfellow, P.N. Nature (1993) [Pubmed]
  2. HMG1 interacts with HOX proteins and enhances their DNA binding and transcriptional activation. Zappavigna, V., Falciola, L., Helmer-Citterich, M., Mavilio, F., Bianchi, M.E. EMBO J. (1996) [Pubmed]
  3. High-mobility-group 1 protein mediates DNA bending as determined by ring closures. Pil, P.M., Chow, C.S., Lippard, S.J. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  4. A bipartite yeast SSRP1 analog comprised of Pob3 and Nhp6 proteins modulates transcription. Brewster, N.K., Johnston, G.C., Singer, R.A. Mol. Cell. Biol. (2001) [Pubmed]
  5. Protein kinase CK2 phosphorylates the high mobility group domain protein SSRP1, inducing the recognition of UV-damaged DNA. Krohn, N.M., Stemmer, C., Fojan, P., Grimm, R., Grasser, K.D. J. Biol. Chem. (2003) [Pubmed]
  6. Isolation of a novel Sry-related gene that is expressed in high-metastatic K-1735 murine melanoma cells. Tani, M., Shindo-Okada, N., Hashimoto, Y., Shiroishi, T., Takenoshita, S., Nagamachi, Y., Yokota, J. Genomics (1997) [Pubmed]
  7. Differential binding of HMG1, HMG2, and a single HMG box to cisplatin-damaged DNA. Farid, R.S., Bianchi, M.E., Falciola, L., Engelsberg, B.N., Billings, P.C. Toxicol. Appl. Pharmacol. (1996) [Pubmed]
  8. Differences in the DNA-binding properties of the HMG-box domains of HMG1 and the sex-determining factor SRY. Teo, S.H., Grasser, K.D., Thomas, J.O. Eur. J. Biochem. (1995) [Pubmed]
  9. Antibodies against a peptide sequence located in the linker region of the HMG-1/2 box domains in sera from patients with juvenile rheumatoid arthritis. Jung, F., Neuer, G., Bautz, F.A. Arthritis Rheum. (1997) [Pubmed]
  10. Alx4 binding to LEF-1 regulates N-CAM promoter activity. Boras, K., Hamel, P.A. J. Biol. Chem. (2002) [Pubmed]
  11. Nature of full-length HMGB1 binding to cisplatin-modified DNA. Jung, Y., Lippard, S.J. Biochemistry (2003) [Pubmed]
  12. Interactions of the basic N-terminal and the acidic C-terminal domains of the maize chromosomal HMGB1 protein. Thomsen, M.S., Franssen, L., Launholt, D., Fojan, P., Grasser, K.D. Biochemistry (2004) [Pubmed]
  13. Formation of large nucleoprotein complexes upon binding of the high-mobility-group (HMG) box B-domain of HMG1 protein to supercoiled DNA. Stros, M., Reich, J. Eur. J. Biochem. (1998) [Pubmed]
  14. HMGB1 and HMGB2 cell-specifically down-regulate the p53- and p73-dependent sequence-specific transactivation from the human Bax gene promoter. Stros, M., Ozaki, T., Bacikova, A., Kageyama, H., Nakagawara, A. J. Biol. Chem. (2002) [Pubmed]
  15. L-Sox5, Sox6 and Sox9 control essential steps of the chondrocyte differentiation pathway. Lefebvre, V., Behringer, R.R., de Crombrugghe, B. Osteoarthr. Cartil. (2001) [Pubmed]
  16. Structural basis for SRY-dependent 46-X,Y sex reversal: modulation of DNA bending by a naturally occurring point mutation. Murphy, E.C., Zhurkin, V.B., Louis, J.M., Cornilescu, G., Clore, G.M. J. Mol. Biol. (2001) [Pubmed]
  17. Structural requirements for cooperative binding of HMG1 to DNA minicircles. Webb, M., Payet, D., Lee, K.B., Travers, A.A., Thomas, J.O. J. Mol. Biol. (2001) [Pubmed]
  18. Solution structure of the first HMG box domain in human upstream binding factor. Xu, Y., Yang, W., Wu, J., Shi, Y. Biochemistry (2002) [Pubmed]
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