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Gene Review

HMGB1  -  high mobility group box 1

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Disease relevance of HMGB1

  • HMG 1 protects 50% of highly negatively supercoiled DNA from E. coli topoisomerase I at a molar ratio of 100:1, and protects all supercoils at a molar ratio of 200:1, indicating saturation of the DNA at this concentration [1].
  • High mobility group protein 1 preferentially conserves torsion in negatively supercoiled DNA [1].

High impact information on HMGB1

  • Autoradiography of thin sections showed that 125I-labeled HMG1 localized within nuclei, and further established that it remained associated with metaphase chromosomes at mitosis [2].
  • Similar results were obtained with bovine fibroblasts, indicating that a dynamic equilibrium exists between HMG1 and chromatin within living cells [2].
  • Here, we show that extracellular HMGB1 and its receptor for advanced glycation end products (RAGE) induce both migration and proliferation of vessel-associated stem cells (mesoangioblasts), and thus may play a role in muscle tissue regeneration [3].
  • Peptides corresponding to the N-terminal, central and central plus C-terminal domains of high mobility group protein HMG-1 from calf thymus have been isolated after digestion in solution with protease V8 under structuring conditions (0.35 M NaCl, pH 7.1) [4].
  • Accordingly, RAGE blockade by neutralizing Abs inhibits HMGB1-induced neovascularization in vivo and endothelial cell proliferation and membrane ruffling in vitro [5].

Biological context of HMGB1


Anatomical context of HMGB1


Associations of HMGB1 with chemical compounds


Other interactions of HMGB1

  • Quantitative microcomplement fixation assays revealed that the indices of dissimilarity between HMG-1 and HMG-2, HMG-3, HMG-8, HMG-14, and HMG-17 were 2.0, 1.0, 3.8, 10.0, and 6.1, respectively [20].
  • These correspond to 6%, 0%, 12%, 20%, and 16% sequence difference between HMG-1 and the other five HMG proteins, although the immunological distance between HMG-1 and HMG-14 may be too large to allow a good correlation between the sequence and the immunological reaction [20].
  • Assignment of syndecan 2 (SDC2)gene to cattle chromosome band 14q22 and thymus high mobility group box protein TOX (TOX)(2) gene to cattle chromosome band 14q17-->q18 by in situ hybridization [21].

Analytical, diagnostic and therapeutic context of HMGB1

  • Based on the analysis of FTIR and UV-CD spectra, the interaction of DNA with nonhistone chromatin protein HMGB1 and linker histone H1 was studied [22].
  • The ternary complex, DNA X HMG1 X 1, seemed to represent a specific structure, since its formation depeNded on the reduced sulfhydryl state of HMG1; the disulfide form of HMG1, which was shown by circular dichroism to contain more random coil than did the reduced form, had no effect on the circular dichroic spectrum of the DNA X H1 complex [23].
  • (iii) Electron microscopy shows that HMG3 at a low protein:DNA input ratio (1:1 w/w; r = 1), and HMG1 at a 6-fold higher ratio, cause looping of relaxed circular DNA at 150 mM ionic strength [24].
  • Oxidized forms of non-histone chromosomal proteins high mobility group 1 (HMG1) and HMG2 were detected by high-pressure liquid chromatography of preparations stored at 4 degrees C for 1 day [25].
  • Western blotting and transcription reconstituted with purified factors show a copurification of HMG-1 and -2 with factor II B, described earlier by Reinberg and Roeder [(1987) J. Biol. Chem. 262, 3310-3321] [26].


  1. High mobility group protein 1 preferentially conserves torsion in negatively supercoiled DNA. Sheflin, L.G., Spaulding, S.W. Biochemistry (1989) [Pubmed]
  2. Microinjection of the nonhistone chromosomal protein HMG1 into bovine fibroblasts and HeLa cells. Rechsteiner, M., Kuehl, L. Cell (1979) [Pubmed]
  3. Extracellular HMGB1, a signal of tissue damage, induces mesoangioblast migration and proliferation. Palumbo, R., Sampaolesi, M., De Marchis, F., Tonlorenzi, R., Colombetti, S., Mondino, A., Cossu, G., Bianchi, M.E. J. Cell Biol. (2004) [Pubmed]
  4. Interaction between domains in chromosomal protein HMG-1. Carballo, M., Puigdomènech, P., Tancredi, T., Palau, J. EMBO J. (1984) [Pubmed]
  5. Cutting edge: extracellular high mobility group box-1 protein is a proangiogenic cytokine. Mitola, S., Belleri, M., Urbinati, C., Coltrini, D., Sparatore, B., Pedrazzi, M., Melloni, E., Presta, M. J. Immunol. (2006) [Pubmed]
  6. Isolation and partial sequence of bovine cDNA clones for the high-mobility-group protein (HMG-1). Pentecost, B., Dixon, G.H. Biosci. Rep. (1984) [Pubmed]
  7. HMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid sequences. Dintilhac, A., Bernués, J. J. Biol. Chem. (2002) [Pubmed]
  8. High mobility group proteins of amphibian oocytes: a large storage pool of a soluble high mobility group-1-like protein and involvement in transcriptional events. Kleinschmidt, J.A., Scheer, U., Dabauvalle, M.C., Bustin, M., Franke, W.W. J. Cell Biol. (1983) [Pubmed]
  9. Phosphorylation of high mobility group protein 14 by casein kinase II. Walton, G.M., Spiess, J., Gill, G.N. J. Biol. Chem. (1985) [Pubmed]
  10. Studies of acetylation and deacetylation in high mobility group proteins. Identification of the sites of acetylation in HMG-1. Sterner, R., Vidali, G., Allfrey, V.G. J. Biol. Chem. (1979) [Pubmed]
  11. Monoclonal antibody against non-histone chromosomal protein high mobility group 1 Co-migrates with high mobility group 1 into the nucleus. Tsuneoka, M., Imamoto, N.S., Uchida, T. J. Biol. Chem. (1986) [Pubmed]
  12. Histone and high mobility group protein phosphorylation in the thyroid: regulation by cyclic nucleotides. Cooper, E., Spaulding, S.W. Endocrinology (1984) [Pubmed]
  13. Regulation of type-II collagen gene expression during human chondrocyte de-differentiation and recovery of chondrocyte-specific phenotype in culture involves Sry-type high-mobility-group box (SOX) transcription factors. Stokes, D.G., Liu, G., Dharmavaram, R., Hawkins, D., Piera-Velazquez, S., Jimenez, S.A. Biochem. J. (2001) [Pubmed]
  14. Differential phosphorylation of high mobility group protein hmg 14 from calf thymus and avian erythrocytes by a cyclic gmp-dependent protein kinase. Palvimo, J., Linnala-Kankkunen, A., Mäenpää, P.H. Biochem. Biophys. Res. Commun. (1983) [Pubmed]
  15. High mobility group proteins 1 and 2 bind preferentially to brominated poly(dG-dC).poly(dG-dC) in the Z-DNA conformation but not to other types of Z-DNA. Christen, T., Bischoff, M., Hobi, R., Kuenzle, C.C. FEBS Lett. (1990) [Pubmed]
  16. Affinity purification of newly phosphorylated protein molecules. Thiophosphorylation and recovery of histones H1, H2B, and H3 and the high mobility group protein HMG-1 using adenosine 5'-O-(3-thiotriphosphate) and cyclic AMP-dependent protein kinase. Sun, I.Y., Johnson, E.M., Allfrey, V.G. J. Biol. Chem. (1980) [Pubmed]
  17. The high mobility group protein 1 enhances binding of the estrogen receptor DNA binding domain to the estrogen response element. Romine, L.E., Wood, J.R., Lamia, L.A., Prendergast, P., Edwards, D.P., Nardulli, A.M. Mol. Endocrinol. (1998) [Pubmed]
  18. The isolation and partial sequence of peptides produced by cyanogen bromide cleavage of calf thymus non-histone chromosomal high-mobility-group protein 2. Sequence homology with non-histone chromosomal high-mobility-group protein 1. Walker, J.M., Gooderham, K., Johns, E.W. Biochem. J. (1979) [Pubmed]
  19. The specific interactions of HMG 1 and 2 with negatively supercoiled DNA are modulated by their acidic C-terminal domains and involve cysteine residues in their HMG 1/2 boxes. Sheflin, L.G., Fucile, N.W., Spaulding, S.W. Biochemistry (1993) [Pubmed]
  20. Immunological relatedness of high mobility group chromosomal proteins from calf thymus. Bustin, M., Hopkins, R.B., Isenberg, I. J. Biol. Chem. (1978) [Pubmed]
  21. Assignment of syndecan 2 (SDC2)gene to cattle chromosome band 14q22 and thymus high mobility group box protein TOX (TOX)(2) gene to cattle chromosome band 14q17-->q18 by in situ hybridization. Goldammer, T., Owens, E., Brunner, R.M., Kata, S.R., Womack, J.E., Schwerin, M. Cytogenet. Genome Res. (2002) [Pubmed]
  22. Fourier transform infrared/vibrational circular dichroism spectroscopy as an informative tool for the investigation of large supramolecular complexes of biological macromolecules. Polyanichko, A., Wieser, H. Biopolymers (2005) [Pubmed]
  23. Non-histone chromosomal protein HMG1 modulates the histone H1-induced condensation of DNA. Kohlstaedt, L.A., Sung, E.C., Fujishige, A., Cole, R.D. J. Biol. Chem. (1987) [Pubmed]
  24. DNA looping by the HMG-box domains of HMG1 and modulation of DNA binding by the acidic C-terminal domain. Stros, M., Stokrová, J., Thomas, J.O. Nucleic Acids Res. (1994) [Pubmed]
  25. Native state of high mobility group chromosomal proteins 1 and 2 is rapidly lost by oxidation of sulfhydryl groups during storage. Kohlstaedt, L.A., King, D.S., Cole, R.D. Biochemistry (1986) [Pubmed]
  26. High mobility group proteins 1 and 2 function as general class II transcription factors. Singh, J., Dixon, G.H. Biochemistry (1990) [Pubmed]
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