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Purification and properties of a cruciform DNA binding protein fromUstilago maydis

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Abstract

A DNA binding protein with an Mr of 11000 was purified fromUstilago maydis. Its solubility in acid, amino acid composition, and mobility during gel electrophoresis are reminiscent of properties observed for the high mobility group nonhistone chromosomal proteins. The protein recognizes cruciform DNA made from oligonucleotides and also binds preferentially to a plasmid containing an extruded cruciform.

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References

  • Bianchi M (1991) Production of functional rat HMG1 protein inEscherichia coli. Gene 104: 271–275

    Google Scholar 

  • Bianchi M, Beltrame M, Paonessa G (1989) Specific recognition of cruciform DNA by nuclear protein HMG1. Science 243: 1056–1059

    Google Scholar 

  • Birnboim HC, Doly J (1979) A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res 7: 1513–1523

    Google Scholar 

  • Bonne C, Duguet M, de Recondo A-M (1980) Single-strand DNA binding protein from rat liver: interactions with supercoiled DNA. Nucleic Acids Res 8: 4955–4968

    Google Scholar 

  • Bonne C, Sautiere P, Duguet M, de Recondo A-M (1982) Identification of a single-stranded DNA binding protein from rat liver with high mobility group protein 1. J Biol Chem 257: 2722–2725

    Google Scholar 

  • Bustin M, Lehn DA, Landsman D (1990) Structural features of the HMG chromosomal proteins and their genes. Biochim Biophys Acta 1049: 231–243

    Google Scholar 

  • Chem Sm, Heffron F, Leupin W, Chazin WJ (1991) Two-dimensional1H NMR studies of synthetic immobile Holliday junctions. Biochemistry 30: 766–771

    Google Scholar 

  • Churchill MEA, Tullius TD, Kallenbach NR, Seeman NC (1988) A Holliday recombination intermediate is twofold symmetric. Proc Natl Acad Sci USA 85: 4653–4656

    Google Scholar 

  • Cooper JP, Hagerman PJ (1987) Gel electrophoretic analysis of the geometry of a DNA four-way junction. J Mol Biol 198: 711–719

    Google Scholar 

  • Cooper JP, Hagerman PJ (1989) Geometry of a branched DNA structure in solution. Proc Natl Acad Sci USA 86: 7336–7340

    Google Scholar 

  • Cunningham RP, DasGupta C, Shibata T, Radding CM (1980) Homologous pairing in genetic recombination: recA protein makes joint molecules of gapped circular DNA and closed circular DNA. Cell 20: 223–235

    Google Scholar 

  • Dixon DA, Kowalczykowski SC (1991) Homologous pairing in vitro stimulated by the recombination hospot, Chi. Cell 66: 361–371

    Google Scholar 

  • Duckett DR, Murchie AIH, Diekmann S, von Kitzing W, Kemper B, Lilley DMJ (1988) The structure of the Holliday junction and its resolution. Cell 55: 79–89

    Google Scholar 

  • Duckett DR, Murchie AIH, Lilley DMJ (1990) The role of metal ions in the conformation of the four-way DNA junction. EMBO J 9: 583–590

    Google Scholar 

  • Dunderdale HJ, Benson FE, Parsons CA, Sharples GJ, Lloyd RG, West SC (1991) Formation and resolution of recombination intermediates byE. coli RecA and RuvC proteins. Nature 354: 506–510

    Google Scholar 

  • Elborough KM, West SC (1988) Specific binding of cruciform DNA structures by a protein from human extracts. Nucleic Acids Res 16: 3603–3616

    Google Scholar 

  • Gellert M, O'Dea MH, Mizuuchi K (1983) Slow cruciform transitions in palindromic DNA. Proc Natl Acad Sci USA 80: 5545–5549

    Google Scholar 

  • Giese K, Cox J, Grosschedl R (1992) The HMG domain of lymphoid enhancer factor 1 bends DNA and facilitates assembly of functional nucleoprotein structures. Cell 69: 185–195

    Google Scholar 

  • Gough GW, Sullivan KM, Lilley DMJ, (1986) The structure of cruciforms in supercoiled DNA: probing the single-stranded character of nucleotide bases with bisulphite. EMBO J 5: 191–196

    Google Scholar 

  • Gubbay J, Collingnon J, Koopman P, Capel B, Economou A, Musterberg A, Vivian N, Goodfellow P, Lovell-Badge R (1990) A gene mapping to the sex-determining region of the mouse Y chromosome is a member of a novel family of embryonically expressed genes. Nature 346: 245–250

    Google Scholar 

  • Holliday R (1964) A mechanism for gene conversion in fungi. Genet Res 5: 282–304

    Google Scholar 

  • Jantzen HM, Admon A, Bell SP, Tjian R (1990) Nucleolar transcription factor hUBF contains a DNA-binding motif with homology to HMG protein. Nature 344: 830–836

    Google Scholar 

  • Javaherian K, Sadegi M, Liu LF (1979) Nonhistone proteins HMG1 and HMG2 unwind DNA double helix. Nucleic Acids Res 6: 3569–3580

    Google Scholar 

  • Johns EW (1982) History, definition and problems. In: Johns EW (ed) The HMG chromosomal proteins. Academic Press, New York, pp. 1–7

    Google Scholar 

  • Kallenbach NR, Ma RI, Seeman NC (1983) An immobile nucleic acid junction constructed from oligonucleotides. Nature 305: 829–831

    Google Scholar 

  • Kmiec E, Holloman WK (1982) Homologous pairing of DNA molecules promoted by a protein fromUstilago. Cell 29: 367–374

    Google Scholar 

  • Kmiec E, Holloman WK (1986) Homologous pairing of DNA molecules byUstilago rec1 protein is promoted by sequences of Z-DNA. Cell 44: 545–554

    Google Scholar 

  • Kolodrubetz D, Burgum A (1990) DuplicatedNHP6 genes ofSacharomyces cerevisiae encode proteins homologous to bovine high mobility group protein 1. J Biol Chem 265: 3234–3239

    Google Scholar 

  • Kruger W, Herskowitz I (1991) A negative regulator of HO transcription,SIN1 (SPT2), is a nonspecific DNA-binding protein related to HMG1. Mol Cell Biol 11: 4135–4146

    Google Scholar 

  • McEntee K, Weinstock GM, Lehman IR (1980) Initiation of general recombination catalyzed in vitro by the recA protein ofE. coli. Proc Natl Acad Sci USA 77: 857–861

    Google Scholar 

  • Murchie AIH, Clegg RM, von Kitzing E, Duckett DR, Diekmann S, Lilley DMJ (1989) Fluorescence energy transfer shows that the four-way DNA junction is a right-handed cross of antiparallel molecules. Nature 341: 763–766

    Google Scholar 

  • Parsons CA, Tsaneva I, Lloyd RG, West SC (1992) Interaction ofEscherichia coli RuvA and RuvB proteins with synthetic Holliday junctions. Proc Natl Acad Sci USA 89: 5452–5456

    Google Scholar 

  • Peterson CL, Kruger W, Herskowitz I (1991) A functional interaction between the C-terminal domain of RNA polymerase II and the negative regulatorSIN1. Cell 64: 1135–1143

    Google Scholar 

  • Radding CM (1991) Helical interactions in homologous pairing and strand exchange driven by RecA protein. J Biol Chem 266: 5355–5358

    Google Scholar 

  • Roeder GS, Beard C, Smith M, Keranen S (1985) Isolation and characterization of theSPT2 gene, a negative regulator of Tycontrolled yeast gene expression. Mol Cell Biol 5: 1543–1553

    Google Scholar 

  • Seeman NC, Kallenbach NR (1983) Design of immobile nucleic acid junctions. Biophys J 44: 201–209

    Google Scholar 

  • Shiba T, Iwasaki H, Nakata A, Shinagawa H (1991) SOS-inducible DNA repair proteins, RuvA and RuvB, ofEscherichia coli: Functional intermediates between RuvA and RuvB for ATP hydrolysis and renaturation of the cruciform structure in supercoiled DNA. Proc Natl Acad Sci USA 88: 8445–8449

    Google Scholar 

  • Singh J, Dixon GH (1990) High mobility group proteins 1 and 2 function as general class II transcription factors. Biochemistry 29: 6295–6302

    Google Scholar 

  • Smith GR (1990) RecBCD enzyme. In: Eckstein F, Lilley DMJ (eds) Nucleic acids and Molecular Biology 4. Springer, Berlin, pp. 78–98

    Google Scholar 

  • Sugimoto A, Iino Y, Maeda T, Watanabe Y, Yamamoto M (1991)Schizosaccharomyces pombe stell + encodes a transcription factor with an HMG motif that is a critical regulator of sexual development. Genes Dev 5: 1990–1999

    Google Scholar 

  • Symington L, Kolodner R (1985) Partial purification of an enzyme fromSaccharomyces cerevisiae that cleaves Holliday junctions. Proc Natl Acad Sci USA 82: 7247–7251

    Google Scholar 

  • Takahagi M, Iwasaki H, Nakata A, Shinagawa H (1991) Molecular analysis of theEscherichia coli ruvC gene which encodes a Holliday junction-specific endonuclease. J Bacteriol 173: 5747–5753

    Google Scholar 

  • Travis A, Amsterdam A, Belanger C, Grosshedl R (1991) LEF-1 a gene encoding a lymphoid specific protein with an HMG domain, regulates T-cell receptor alpha enhancer function. Genes Dev 5: 880–894

    Google Scholar 

  • Tsaneva IR, Muller B, West SC (1992) ATP-dependent branch migration of Holliday junctions promoted by the RuvA and RuvB proteins ofE. coli Cell 69: 1171–1180

    Google Scholar 

  • van de Sande JH, Kleppe K, Khorana HG (1973) Reversal of bacteriophage T4 induced polynucleotide kinase action. Biochemistry 12: 5050–5055

    Google Scholar 

  • van de Wetering M, Oosterwegel M, Dooijes D, Clevers H (1991) Identification and cloning of TCF-1, a T-lymphocyte-specific transcription factor containing a sequence specific HMG box. EMBO J 10: 123–132

    Google Scholar 

  • Waga S, Mizuno S, Yoshida M (1990) Chromosomal protein HMG1 removes the transcriptional block caused by the cruciform in supercoiled DNA. J Biol Chem 265: 19424–19428

    Google Scholar 

  • Warren GJ, Green RL (1985) Comparison of physical and genetic properties of palindromic DNA sequences. J Bacteriol 161: 1103–1111

    Google Scholar 

  • Weber S, Isenberg I (1980) High mobility group proteins ofSaccharomyces cerevisiae. Biochemistry 19: 2236–2240

    Google Scholar 

  • Wemmer DE, Wand AJ, Seeman NC, Kallenbach NR (1985) NMR analysis of DNA junctions: imino proton NMR studies of individual arms and intact junction. Biochemistry 24: 5745–5749

    Google Scholar 

  • West SC (1992) Enzymes and molecular mechanisms of genetic recombination. Annu Rev Biochem 61: 603–640

    Google Scholar 

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Authors and Affiliations

  1. Department of Pharmacology, Jefferson Cancer Institute, Thomas Jefferson University, 19107, Philadelphia, PA, USA

    H. Kotani & E. B. Kmiec

  2. Department of Microbiology, Cornell University Medical College, 1300 York Avenue, 10021, New York, NY, USA

    W. K. Holloman

Authors
  1. H. Kotani
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  2. E. B. Kmiec
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  3. W. K. Holloman
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Communicated by: P.B. Moens

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Kotani, H., Kmiec, E.B. & Holloman, W.K. Purification and properties of a cruciform DNA binding protein fromUstilago maydis . Chromosoma 102, 348–354 (1993). https://doi.org/10.1007/BF00661278

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  • DOI: https://doi.org/10.1007/BF00661278

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