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Gene Review

HMGN2  -  high mobility group nucleosomal binding...

Homo sapiens

Synonyms: HMG17, High mobility group nucleosome-binding domain-containing protein 2, Non-histone chromosomal protein HMG-17
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Disease relevance of HMGN2

  • Upon i.v. injection, phage displaying this HMGN2 fragment homed to HL-60 and MDA-MB-435 tumors [1].
  • 1. Because this region is frequently involved in chromosomal aberrations of various human neoplasms, two PAC clones containing an HMG17 sequence were isolated [2].
  • The antimicrobial assays showed that the Escherichia coli-based production of HMGN2 had a potent antimicrobial activity against E. coli ML-35p, Pseudomonas aeruginosa ATCC 27853, and to some extent, against Candida albicans ATCC 10231 [3].
  • The antimicrobial assay showed that the MIC of the recombinant holo-HMGN2 against E coli ML-35p (an ampicillin-resistance strain), Pseudomonas aeruginosa ATCC 27853 and Candida albicans ATCC 10231 were 12.5, 25, and 100 mg/L, respectively [4].
  • In contrast, recombinant holo-HMGN2 was inactive against Staphylococcus aureus ATCC 25923 [4].

High impact information on HMGN2


Biological context of HMGN2


Anatomical context of HMGN2

  • Chromosomal high-mobility-group (HMG) proteins have been examined as substrates for calcium/phospholipid-dependent protein kinase C. Protein kinase C from rat brain phosphorylated efficiently both HMG 14 and HMG 17 derived from calf thymus and the reactions were calcium/phospholipid-dependent [13].
  • When in vivo [32P] phosphate labeled HMG proteins from unsynchronized HeLa cells are separated by electrophoresis in acid-urea polyacrylamide gels, as opposed to separation in SDS-polyacrylamide, HMG 17 does not show any 32P incorporation [14].
  • Our results indicate that HMG-17 was not phosphorylated in human colon carcinoma cell line HT-29 incubated for 18 h with 32Pi, but that HMG-14a and HMG-14b were phosphorylated [15].
  • HMGN2: a novel antimicrobial effector molecule of human mononuclear leukocytes [3]?
  • The results suggest that COS cells can tolerate large excess of HMG mRNAs and protein, that the relative amounts of HMG-14 and HMG-17 and their mRNAs are not constant, and that neither the transcription nor the translation of the proteins is coordinately regulated [16].

Associations of HMGN2 with chemical compounds


Physical interactions of HMGN2

  • Third, by comparing the full-length protein with different domains, we demonstrate that the acidic carboxyl-terminal domain is absolutely required for nucleosome spacing, neither the nucleosome binding domain of HMG 14 or HMG 17 nor the amino-terminal domain plus the nucleosome binding domain of HMG 14 could space nucleosomes [11].
  • A large part of exon 8 of the D-PCa-2 gene shows strong similarity to the high-mobility-group nucleosomal binding protein 2 (HMGN2) cDNA [21].

Enzymatic interactions of HMGN2

  • In order to definitively determine whether HMG-17 is indeed phosphorylated or whether the protein previously identified as [32P]HMG-17 was a subgroup of HMG-14, we have used the technique of electroblotting in conjunction with an immunochemical procedure utilizing anti-HMG-17 IgG [15].

Regulatory relationships of HMGN2


Other interactions of HMGN2


Analytical, diagnostic and therapeutic context of HMGN2


  1. A fragment of the HMGN2 protein homes to the nuclei of tumor cells and tumor endothelial cells in vivo. Porkka, K., Laakkonen, P., Hoffman, J.A., Bernasconi, M., Ruoslahti, E. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  2. Regional fine mapping of HMG17 to chromosomal band 1p35. Kazmierczak, B., Dal Cin, P., Rogalla, P., Van den Berghe, H., Bullerdiek, J. Cancer Genet. Cytogenet. (2000) [Pubmed]
  3. HMGN2: a novel antimicrobial effector molecule of human mononuclear leukocytes? Feng, Y., Huang, N., Wu, Q., Wang, B. J. Leukoc. Biol. (2005) [Pubmed]
  4. Alpha-helical domain is essential for antimicrobial activity of high mobility group nucleosomal binding domain 2 (HMGN2). Feng, Y., Huang, N., Wu, Q., Bao, L., Wang, B.Y. Acta Pharmacol. Sin. (2005) [Pubmed]
  5. Autoantibodies to nucleosomal proteins: antibodies to HMG-17 in autoimmune diseases. Bustin, M., Reisch, J., Einck, L., Klippel, J.H. Science (1982) [Pubmed]
  6. Chromosomal proteins HMG-14 and HMG-17 are released from mitotic chromosomes and imported into the nucleus by active transport. Hock, R., Scheer, U., Bustin, M. J. Cell Biol. (1998) [Pubmed]
  7. Inhibition of transcription in somatic cells by microinjection of antibodies to chromosomal proteins. Einck, L., Bustin, M. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  8. HMGN3a and HMGN3b, two protein isoforms with a tissue-specific expression pattern, expand the cellular repertoire of nucleosome-binding proteins. West, K.L., Ito, Y., Birger, Y., Postnikov, Y., Shirakawa, H., Bustin, M. J. Biol. Chem. (2001) [Pubmed]
  9. Differential phosphorylation of nuclear nonhistone high mobility group proteins HMG 14 and HMG 17 during the cell cycle. Bhorjee, J.S. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  10. Specific acetylation of chromosomal protein HMG-17 by PCAF alters its interaction with nucleosomes. Herrera, J.E., Sakaguchi, K., Bergel, M., Trieschmann, L., Nakatani, Y., Bustin, M. Mol. Cell. Biol. (1999) [Pubmed]
  11. High mobility group protein 14 and 17 can prevent the close packing of nucleosomes by increasing the strength of protein contacts in the linker DNA. Tremethick, D.J., Hyman, L. J. Biol. Chem. (1996) [Pubmed]
  12. Chromosomal protein HMG-14. Complete human cDNA sequence and evidence for a multigene family. Landsman, D., Srikantha, T., Westermann, R., Bustin, M. J. Biol. Chem. (1986) [Pubmed]
  13. Phosphorylation of high-mobility-group chromatin proteins by protein kinase C from rat brain. Palvimo, J., Mahonen, A., Mäenpää, P.H. Biochim. Biophys. Acta (1987) [Pubmed]
  14. Is high mobility group protein 17 phosphorylated in vivo? Re-examination of the HeLa cell cycle data. Bhorjee, J.S., Mellon, I., Kifle, L. Biochem. Biophys. Res. Commun. (1983) [Pubmed]
  15. Evidence that high mobility group protein 17 is not phosphorylated in human colon carcinoma cells. Chapekar, M.S., Bustin, M., Glazer, R.I. Biochim. Biophys. Acta (1985) [Pubmed]
  16. Modulation of the cellular ratio of chromosomal high mobility group proteins 14 to 17 in transfected cells. Giri, C., Landsman, D., Soares, N., Bustin, M. J. Biol. Chem. (1987) [Pubmed]
  17. The effect of a high mobility group protein (HMG 17) on the structure of acetylated and control core HeLa cell chromatin. Sasi, R., Fasman, G.D. Biochim. Biophys. Acta (1984) [Pubmed]
  18. Chromosomal proteins HMG-14 and HMG-17. Distinct multigene families coding for similar types of transcripts. Landsman, D., Bustin, M. J. Biol. Chem. (1986) [Pubmed]
  19. High mobility group protein 17 cross-links primarily to histone H2A in the reconstituted HMG 17-nucleosome core particle complex. Cook, G.R., Yau, P., Yasuda, H., Traut, R.R., Bradbury, E.M. J. Biol. Chem. (1986) [Pubmed]
  20. Studies of acetylation and deacetylation in high mobility group proteins. Identification of the sites of acetylation in high mobility group proteins 14 and 17. Sterner, R., Vidali, G., Allfrey, V.G. J. Biol. Chem. (1981) [Pubmed]
  21. D-PCa-2: a novel transcript highly overexpressed in human prostate and prostate cancer. Weigle, B., Kiessling, A., Ebner, R., Fuessel, S., Temme, A., Meye, A., Schmitz, M., Rieger, M.A., Ockert, D., Wirth, M.P., Rieber, E.P. Int. J. Cancer (2004) [Pubmed]
  22. HMGN4, a newly discovered nucleosome-binding protein encoded by an intronless gene. Birger, Y., Ito, Y., West, K.L., Landsman, D., Bustin, M. DNA Cell Biol. (2001) [Pubmed]
  23. Mapping the human gene coding for chromosomal protein HMG-17. Popescu, N., Landsman, D., Bustin, M. Hum. Genet. (1990) [Pubmed]
  24. Chromosomal proteins HMG-14 and HMG-17 are synthesized throughout the S-phase in Burkitt's lymphoma. Morton, R.L., David, H., O'Connor, P.M., Bustin, M. Biochem. Biophys. Res. Commun. (1996) [Pubmed]
  25. Phosphorylation and subcellular redistribution of high mobility group proteins 14 and 17, analyzed by mass spectrometry. Louie, D.F., Gloor, K.K., Galasinski, S.C., Resing, K.A., Ahn, N.G. Protein Sci. (2000) [Pubmed]
  26. Nucleosome core binding region of chromosomal protein HMG-17 acts as an independent functional domain. Crippa, M.P., Alfonso, P.J., Bustin, M. J. Mol. Biol. (1992) [Pubmed]
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