High affinity MAR-DNA binding is a common property of murine and human mutant p53

Journal of Cellular Biochemistry

Volumn 69, Issue 3, 1998, Pages 260-270

  Will, Katrin ^a   Warnecke, Gabriele ^a   Albrechtsen, Nils ^a   Boulikas, Teni ^b   Deppert, Wolfgang ^a  

^a UNIVERSITY OF HAMBURG   (Germany)

^b Inst of Molecular Medical Sciences   (United States)

Author keywords

MAR DNA binding by mutant p53; MAR DNA elements; MethA p53; Oncogenic function of mutant p53

Indexed keywords

PROTEIN P53;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; ENHANCER REGION; GENE LOCUS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DNA BINDING;

3T3 CELLS; ANIMALS; DNA; DNA FRAGMENTATION; HUMANS; MICE; MICE, INBRED BALB C; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; RECOMBINANT PROTEINS; TUMOR SUPPRESSOR PROTEIN P53;

EID: 0032104865     PISSN: 07302312     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4644(19980601)69:3<260::AID-JCB4>3.0.CO;2-P     Document Type: Article

References (31)

1. Bakalkin G, Selivanova G, Yakovleva T, Kiseleva E, Kashuba E, Magnusson KP, Szekely L, Klein G, Terenius L, Wiman KG (1995): p53 binds single-stranded DNA ends through the C-terminal domain and internal DNA segments via the middle domain. Nucleic Acids Res 23: 362-369.
2. Bode J, Maaβ K (1988): Chromatin domain surrounding the human interferon-beta gene as defined by scaffold-attached regions. Biochemistry 27:4706-4711.
3. Boulikas T (1995a): Chromatin domains and prediction of MAR sequences. Int Rev Cytol 162A:279-388.
4. Boulikas T (1995b): How enhancers work: Juxtapositioning of DNA control elements by synergistic interaction of MARs. Int J Oncol 6:1313-1318.
5. Boulikas T, Kong CF (1993): Multitude of inverted repeats characterizes a class of anchorage sites of chromatin loops to the nuclear matrix. J Cell Biochem 53:1-12.
6. Boulikas T, Kong CF, Brooks D, Hsie L (1996): The 3′ untranslated region of the human poly(ADP-ribose) polymerase gene is anchored to the nuclear matrix. Int J Oncol 9:1287-1294.
7. Cockerill PN, Yuen M-H, Garrard WT (1987): The enhancer of the immunglubulin heavy chain locus is flanked by presumptive chromosomal loop anchorage elements. J Biol Chem 262:5394-5397.
8. Cox LS, Lane DP, (1995): Tumour suppressors, kinases and clamps: How p53 regulates the cell cycle in response to DNA damage. Bioessays 17:501-508.
9. DeLeo AB, Shiku H, Takahashi T, John M, Old LJ (1977): Cell surface antigens of chemically induced sarcomas of the mouse. I. Murine leukemia virus-related antigens and alloantigens on cultured fibroblasts and sarcoma cells: Description of a unique antigen on BALB/c Meth A sarcoma. J Exp Med 146:720-734.
10. Deppert W (1994): The yin and yang of p53 in cellular proliferation. Cancer Biol 5:187-202.
11. Deppert W (1996): Binding of MAR-DNA elements by mutant p53: Possible implications for its oncogenic functions. J Cell Biochem 62:172-180.
12. Hainaut P, Soussi T, Shomer B, Hollstein M, Greenblatt M, Hovig E, Harris CC, Montesano R (1997): Database of p53 gene somatic mutations in human tumors and cell lines: Updated compilation and future prospects. Nucleic Acids Res 25:151-157.
13. Hollstein M, Shomer B, Greenblatt M, Soussi T, Hovig E, Montesano R, Harris CC (1996): Somatic point mutations in the p53 gene of human tumors and cell lines: Updated compilation. Nucleic Acids Res 24:141-146.
14. Kern SE, Kinzler KW, Bruskin A, Jarosz D, Friedman P, Prives C, Vogelstein B (1991): Identification of p53 as a sequence-specific DNA-binding protein. Science 252: 1708-1711.
15. Kolzau T, Deppert W (1993): Wild-type p53 in cellular transformation: A reassessment. Int J One 3:23-27.
16. Lin J, Teresky AK, Levine AJ (1995): Two critical hydrophobic amino acids in the N-terminal domain of the p53 protein are required for the gain of function phenotypes of human p53 mutants. Oncogene 10:2387-2390.
17. McKay R (1981): Binding of an SV40 T antigen-related protein to the DNA of SV40 regulatory mutants. Nature 289:810-813.
18. Milner J, Cook A (1986): The cellular tumour antigen p53: Evidence for transformation-related, immunological variants of p53. Virology 154:21-30.
19. Milner J, Medcalf EA (1991): Cotranslation of activated mutant p53 with wild-type drives the wild-type p53 protein into the mutant conformation. Cell 65:765-774.
20. Milner J, Chan YS, Medcalf EA, Eckhart W (1993): Partially transformed T3T3 cells express high levels of mutant p53 in the "wild-type" immunoreactive form with defective oligomerization. Oncogene 8:2001-2008.
21. Müller BF, Paulsen D, Deppert W (1996): Specific binding of MAR/SAR DNA-elements by mutant p53. Oncogene 12:1941-1952.
22. Mummenbrauer T, Janus F, Mueller B, Wiesmueller L, Deppert W, Grosse F (1996): p53 protein exhibits 3′-to-5′ exonuclease activity. Cell 85:1089-1099.
23. Ory K, Legros Y, Auguin C, Soussi T (1994): Analysis of the most representative tumour-derived p53 mutants reveals that changes in protein conformation are nor correlated with loss of transactivation or inhibition of cell proliferation. EMBO J 13:3496-3504.
24. Soussi T, May P (1996): Structural aspects of the p53 protein in relation to gene evolution: A second look. J Mol Biol 260:623-637.
25. Staufenbiel M, Deppert W (1983): Nuclear matrix preparations from liver tissue and from cultured vertebrate cells: Differences in major polypeptides. Eur J Cell Biol 31: 341-348.
26. Steinmeyer K, Deppert W (1988): DNA binding properties of murine p53. Oncogene 3:501-507.
27. Studier FW, Rosenberg AH, Dunn JJ, Dubendorf JW (1990): Use of T7 RNA polymerase to direct expression of clones genes. Methods Enzymol 185:60-89.
28. Vogelstein B, Kinzler KW (1992): p53 function and dysfunction. Cell 70:523-526.
29. von Kries JP, Buhrmester H, Strätling WH (1991): A matrix/ scaffold attachment region binding protein: Identification, purification, and mode of binding. Cell 64:123-135.
30. Weiβker S, Müller B, Homfeld A, Deppert W (1992): Specific and complex interactions of murine p53 with DNA. Oncogene 7:1921-1932.
31. Yewdell JW, Gannon JV, Lane DP (1986): Monoclonal antibody analysis of p53 expression in normal and transformed cells. J Virol 59:444-452.