Advanced SearchSearch Tips
Non-histone protein HMGB1 inhibits the repair of damaged DNA by cisplatin in NIH-3T3 murine fibroblasts
facebook(new window)  Pirnt(new window) E-mail(new window) Excel Download
  • Journal title : BMB Reports
  • Volume 49, Issue 2,  2016, pp.99-104
  • Publisher : Korean Society for Biochemistry and Molecular Biology
  • DOI : 10.5483/BMBRep.2016.49.2.238
 Title & Authors
Non-histone protein HMGB1 inhibits the repair of damaged DNA by cisplatin in NIH-3T3 murine fibroblasts
Yusein-Myashkova, Shazie; Ugrinova, Iva; Pasheva, Evdokia;
  PDF(new window)
The nuclear non-histone protein high mobility group box (HMGB) 1 is known to having an inhibitory effect on the repair of DNA damaged by the antitumor drug cisplatin in vitro. To investigate the role of HMGB1 in living cells, we studied the DNA repair of cisplatin damages in mouse fibroblast cell line, NIH-3T3. We evaluated the effect of the post-synthetic acetylation and C-terminal domain of the protein by overexpression of the parental and mutant GFP fused forms of HMGB1. The results revealed that HMGB1 had also an inhibitory effect on the repair of cisplatin damaged DNA in vivo. The silencing of HMGB1 in NIH-3T3 cells increased the cellular DNA repair potential. The increased levels of repair synthesis could be "rescued" and returned to less than normal levels if the knockdown cells were transfected with plasmids encoding HMGB1 and HMGB1 K2A. In this case, the truncated form of HMGB1 also exhibited a slight inhibitory effect.
Acetylation;Cisplatin;HMGB1;NER;Tail-less HMGB1 protein;
 Cited by
Identification of specifically activated angiogenic molecules in HMGB-1-induced angiogenesis, BMB Reports, 2017, 50, 11, 590  crossref(new windwow)
Goodwin GH, Sanders C and Johns EW (1973) A new group of chromatin-associated proteins with a high content of acidic and basic amino acids. Eur J Biochem 38, 14-19 crossref(new window)

Reeves R and Adair JE (2005) Role of high mobility group (HMG) chromatin proteins in DNA repair. DNA Repair 4, 926-938 crossref(new window)

Pasheva EA, Pashev IG and Favre A (1998) Preferential binding of high mobility group 1 protein to UV damaged DNA. J Biol Chem 273, 24730-24736 crossref(new window)

Pil PM and Lippard SJ (1992) Specific binding of chromosomal protein HMG1 to DNA damaged by the anticancer drug cisplatin. Science 256, 234-237 crossref(new window)

Hughes EN, Engelsberg BN and Billings PC (1992) Purification of nuclear proteins that bind to cisplatin-damaged DNA. Identity with high mobility group proteins 1 and 2. J Biol Chem 267, 13520-13527

Mitkova E, Ugrinova I, Pashev I and Pasheva E (2005) The inhibitory effect of HMGB1 protein on the repair of cisplatin damaged DNA is accomplished through the acidic domain. Biochemistry 44, 5893-5898 crossref(new window)

Lange SS, Reddy MC and Vasquez KM (2009) Human HMGB1 directly facilitates interactions between nucleotide excision repair proteins on triplex-directed psoralen interstrand crosslinks. DNA Repair 8, 865-72 crossref(new window)

Reddy MC, Christensen J and Vasquez KM (2005) Interplay between human high mobility group protein 1 and replication protein A on psoralen-cross-linked DNA. Biochemistry 44, 4188-4195 crossref(new window)

Huang JC, Zamble DB, Reardon RT et al (1994) HMG-domain proteins specifically inhibit the repair of the major DNA adduct of the anticancer drug cisplatin by human excision nuclease. Proc Natl Acad Sci U S A 91, 10394-10398 crossref(new window)

Malina J, Kasparkova J, Natile G and Brabec V (2002) Recognition of major DNA adducts of enantiomeric cisplatin analogs by HMG box proteins and nucleotide excision repair of these adducts. Chem Biol 9, 629-638 crossref(new window)

Patrick SM and Turchi JJ (1998) Human replication protein A preferentially binds cisplatin-damaged duplex DNA in vitro. Biochemistry 37, 8808-8815 crossref(new window)

Zamble DB, Mu D, Reardon JT et al (1996) Repair of cisplatin-DNA adducts by the mammalian excision nuclease. Biochemistry 35, 10004-10013 crossref(new window)

Trimmer EE and Essigmann JM (1998) Human testis-determining factor SRY binds to the major DNA adducts of cisplatin and a putative target sequence with comparable affinities. Biochemistry 37, 352-362 crossref(new window)

Lange SS, Mitchell DL and Vasquez KM (2008) High mobility group protein B1 enhances DNA repair and chromatin modification after DNA damage. Proc Natl Acad Sci U S A 105 (30), 10320-10325 crossref(new window)

Jayaraman L, Moorthy NC, Murthy KG et al (1998) High mobility group protein-1 (HMG-1) is a unique activator of p53. Genes Dev 12, 462-472 crossref(new window)

Banerjee S and Kundu TK (2003) The acidic C-terminal domain and A-box of HMGB-1 regulates p53-mediated transcription. Nucleic Acids Res 31, 3236-3247 crossref(new window)

Stros M, Muselikova-Polanska E, Pospisilova S and Strauss F (2004) High-affinity binding of tumor-suppressor protein p53 and HMGB1 to hemicatenated DNA loops. Biochemistry 43, 7215-7225 crossref(new window)

Smith ML, Ford JM, Hollander MC et al (2000) p53-mediated DNA repair responses to UV radiation: studies of mouse cells lacking p53, p21, and/or gadd45 genes. Mol Cell Biol 20, 3705-3714 crossref(new window)

Rubbi CP and Milner J (2003) p53 is a chromatin accessibility factor for nucleotide excision repair of DNA damage. EMBO J 22, 975-986 crossref(new window)

Huang J, Ni J, Liu K et al (2012) HMGB1 Promotes Drug Resistance in Osteosarcoma. Cancer Res 72, 230-238 crossref(new window)

Ugrinova I, Pasheva EA, Armengaud J and Pashev IG (2001) In vivo acetylation of HMG1 protein enhances its binding affinity to distorted DNA structures. Biochemistry 40, 14655-14660 crossref(new window)

Assenberg R, Webb M, Connolly E et al (2008) A critical role in structure-specific DNA binding for the acetylatable lysine residues in HMGB1. Biochem J 411, 553-561 crossref(new window)

Ueda T, Chou H, Kawase T et al (2004) Acidic C-tail of HMGB1 is required for its target binding to nucleosome linker DNA and transcription stimulation. Biochemistry 43, 9901-9908 crossref(new window)

Knapp S, Muller S, Digilio G et al (2004) The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. Biochemistry 43, 11992-11997 crossref(new window)

Watson M, Stott K, Thomas JO (2007) Mapping intramolecular interactions between domains in HMGB1 using a tail-truncation approach. J Mol Biol 374, 1286-1297 crossref(new window)

Stott K, Watson M, Howe FS et al (2010) Tail-mediated collapse of HMGB1 is dynamic and occurs via differential binding of the acidic tail to the A and B domains. J Mol Biol 403, 706-722 crossref(new window)

Štros M and Vorlíčková M (1990) Non-histone chromosomal protein HMG1 reduces the histone H5-induced changes in c.d. spectra of DNA: the acidic C-terminus of HMG1 is necessary for binding to H5. Int. J Biol Macromol 12, 282-288 crossref(new window)

Cato L, Stott K, Watson M and Thomas JO (2008) The interaction of HMGB1 and linker histones occurs through their acidic and basic tails. J Mol Biol 384, 1262-1272 crossref(new window)

Sutrias-Grau M, Bianchi ME and Bernues J (1999) High mobility group protein 1 interacts specifically with the core domain of human TATA box-binding protein and interferes with transcription factor IIB within the pre-initiation complex. J Biol Chem 274, 1628-1634 crossref(new window)

Das D and Scovell WM (2001) The binding interaction of HMG-1 with the TATA-binding protein/TATA complex. J Biol Chem 276, 32597-32605 crossref(new window)

Ge H and Roeder RG (1994) The high mobility group protein HMG1 can reversibly inhibit class II gene transcription by interaction with the TATA-binding protein. J Biol Chem 269, 17136-17140

Bonaldi T, Längst G, Strohner R et al (2002) The DNA chaperone HMGB1 facilitates ACF/CHRAC-dependent nucleosome sliding. EMBO J 21, 6865-73 crossref(new window)

Cereghini S and Yaniv M (1984) Assembly of transfected DNA into chromatin: Structural changes in the origin-promoter-enhancer region upon replication. EMBO J 3, 1243-1253

Ford JM and Hanawalt PC (1995) Li-Fraumeni syndrome fibroblasts homozygous for p53 mutations are deficient in global DNA repair but exhibit normal transcription-coupled repair and enhanced UV resistance. Proc Natl Acad Sci U S A 92, 8876-8880 crossref(new window)

Hwang BJ, Ford JM, Hanawalt PC and Chu G (1999) Expression of the p48 xeroderma pigmentosum gene is p53-dependent and is involved in global genomic repair. Proc Natl Acad Sci U S A 96, 424-428 crossref(new window)

Fitch ME, Cross IV, Turner SJ et al (2003) The DDB2 nucleotide excision repair gene product p48 enhances global genomic repair in p53 deficient human fibroblasts. DNA Repair 2, 819-826 crossref(new window)

Banerjee S, de Freitas A, Friggeri A, Zmijewski JW, Liu G and Abraham E (2011) Intracellular HMGB1 negatively regulates efferocytosis. J Immunol 187, 4686-4694 crossref(new window)