메뉴 건너뛰기




Volumn 125, Issue 2, 1999, Pages 399-405

The stabilized structural array of two HMG1/2-boxes endowed by a linker sequence between them is requisite for the effective binding of HMG1 with DNA

Author keywords

HMG1; HMG1 2 box; Model building; Mutagenesis; Protein DNA interaction

Indexed keywords

DNA BINDING PROTEIN; HIGH MOBILITY GROUP PROTEIN;

EID: 0033065073     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022300     Document Type: Article
Times cited : (25)

References (48)
  • 1
    • 0025323711 scopus 로고
    • Structural features of the HMG chromosomal proteins and their genes
    • Bustin, M., Lehn, D.A., and Landsman, D. (1990) Structural features of the HMG chromosomal proteins and their genes. Biochim. Biophys. Acta 1049, 231-243
    • (1990) Biochim. Biophys. Acta , vol.1049 , pp. 231-243
    • Bustin, M.1    Lehn, D.A.2    Landsman, D.3
  • 2
    • 0027646025 scopus 로고
    • A signature for the HMG-1 box DNA binding proteins
    • Landsman, D. and Bustin, M. (1993) A signature for the HMG-1 box DNA binding proteins. BioEssays 15, 539-546
    • (1993) BioEssays , vol.15 , pp. 539-546
    • Landsman, D.1    Bustin, M.2
  • 3
    • 0030358586 scopus 로고    scopus 로고
    • High-mobility-group chromosomal proteins: Architectural components that facilitate chromatin function
    • Bustin, M. and Reeves, R. (1996) High-mobility-group chromosomal proteins: architectural components that facilitate chromatin function. Prog. Nucleic Acid Res. Mol. Biol. 54, 35-100
    • (1996) Prog. Nucleic Acid Res. Mol. Biol. , vol.54 , pp. 35-100
    • Bustin, M.1    Reeves, R.2
  • 4
    • 0023705812 scopus 로고
    • Primary structure of non-histone protein HMG1 revealed by the nucleotide sequence
    • Tsuda, K., Kikuchi, M., Mori, K., Waga, S., and Yoshida, M. (1988) Primary structure of non-histone protein HMG1 revealed by the nucleotide sequence. Biochemistry 27, 6159-6163
    • (1988) Biochemistry , vol.27 , pp. 6159-6163
    • Tsuda, K.1    Kikuchi, M.2    Mori, K.3    Waga, S.4    Yoshida, M.5
  • 5
    • 0028580511 scopus 로고
    • Stimulation of transcription in cultured cells by high mobility group protein 1: Essential role of the acidic carboxyl-terminal region
    • Aizawa, S., Nishino, H., Saito, K., Kimura, K., Shirakawa, H., and Yoshida, M. (1994) Stimulation of transcription in cultured cells by high mobility group protein 1: Essential role of the acidic carboxyl-terminal region. Biochemistry 33, 14690-14695
    • (1994) Biochemistry , vol.33 , pp. 14690-14695
    • Aizawa, S.1    Nishino, H.2    Saito, K.3    Kimura, K.4    Shirakawa, H.5    Yoshida, M.6
  • 6
    • 0028966425 scopus 로고
    • Stimulation of transcription accompanying relaxation of chromatin structure in cells overexpressing high mobility group 1 protein
    • Ogawa, Y., Aizawa, S., Shirakawa, H., and Yoshida, M. (1995) Stimulation of transcription accompanying relaxation of chromatin structure in cells overexpressing high mobility group 1 protein. J. Biol. Chem. 270, 9272-9280
    • (1995) J. Biol. Chem. , vol.270 , pp. 9272-9280
    • Ogawa, Y.1    Aizawa, S.2    Shirakawa, H.3    Yoshida, M.4
  • 7
    • 0025280048 scopus 로고
    • Nuclear transcription factor hUBF contains a DNA binding motif with homology to HMG proteins
    • Jantzen, H.M., Admon, A., Bell, S.P., and Tjian, R. (1990) Nuclear transcription factor hUBF contains a DNA binding motif with homology to HMG proteins. Nature 344, 830-836
    • (1990) Nature , vol.344 , pp. 830-836
    • Jantzen, H.M.1    Admon, A.2    Bell, S.P.3    Tjian, R.4
  • 9
    • 0025794148 scopus 로고
    • LEF-1, a gene encoding a lymphoid-specific protein with an HMG domain, regulates T-cell receptor a-enhancer function
    • Travis, A., Amsterdam, A., Belanger, C., and Grosschedl, R. (1991) LEF-1, a gene encoding a lymphoid-specific protein with an HMG domain, regulates T-cell receptor a-enhancer function. Genes Dev. 5, 880-894
    • (1991) Genes Dev. , vol.5 , pp. 880-894
    • Travis, A.1    Amsterdam, A.2    Belanger, C.3    Grosschedl, R.4
  • 10
    • 0025829045 scopus 로고
    • Similarity of human mitochondrial transcription factor 1 to high mobility group proteins
    • Parisi, M.A. and Clayton, D.A. (1991) Similarity of human mitochondrial transcription factor 1 to high mobility group proteins. Science 252, 965-969
    • (1991) Science , vol.252 , pp. 965-969
    • Parisi, M.A.1    Clayton, D.A.2
  • 11
    • 0000113329 scopus 로고
    • HMGs everywhere
    • Ner, S.S. (1992) HMGs everywhere. Curr. Biol. 2, 208-210
    • (1992) Curr. Biol. , vol.2 , pp. 208-210
    • Ner, S.S.1
  • 12
    • 0028197368 scopus 로고
    • HMG domain proteins: Architectural elements in the assembly of nucleoprotein structures
    • Grosschedl, R., Giese, K., and Pagel, J. (1994) HMG domain proteins: architectural elements in the assembly of nucleoprotein structures. Trends Genet. 10, 94-100
    • (1994) Trends Genet. , vol.10 , pp. 94-100
    • Grosschedl, R.1    Giese, K.2    Pagel, J.3
  • 13
    • 0029584667 scopus 로고
    • Solution structure of the sequence-specific HMG box of the lymphocyte transcriptional activator Sox-4
    • van Houte, L.P., Chuprina, V.P., van der Wetering, M., Boelens, R., Kaptein, R., and Clevers, H. (1995) Solution structure of the sequence-specific HMG box of the lymphocyte transcriptional activator Sox-4. J. Biol. Chem. 270, 30516-30524
    • (1995) J. Biol. Chem. , vol.270 , pp. 30516-30524
    • Van Houte, L.P.1    Chuprina, V.P.2    Van Der Wetering, M.3    Boelens, R.4    Kaptein, R.5    Clevers, H.6
  • 14
    • 0029075461 scopus 로고
    • Molecular basis of human 46X, Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex
    • Werner, M.H., Huth, J.R., Gronenborn, A.M., and Clore, G.M. (1995) Molecular basis of human 46X, Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex. Cell 81, 705-714
    • (1995) Cell , vol.81 , pp. 705-714
    • Werner, M.H.1    Huth, J.R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 15
    • 0029131298 scopus 로고
    • Structural basis for DNA bending by the architectural transcription factor LEF-1
    • Love, J.J., Li, X., Case, D.A., Giese, K., Grosschedl, R., and Wright, P.E. (1995) Structural basis for DNA bending by the architectural transcription factor LEF-1. Nature 376, 791-795
    • (1995) Nature , vol.376 , pp. 791-795
    • Love, J.J.1    Li, X.2    Case, D.A.3    Giese, K.4    Grosschedl, R.5    Wright, P.E.6
  • 16
    • 0018267932 scopus 로고
    • Purification from cultured hepatoma cells of two nonhistone chromatin proteins with preferential affinity for single-stranded DNA
    • Bidney, D.L. and Reeck, G.R. (1978) Purification from cultured hepatoma cells of two nonhistone chromatin proteins with preferential affinity for single-stranded DNA. Biochem. Biophys. Res. Commun. 85, 1211-1218
    • (1978) Biochem. Biophys. Res. Commun. , vol.85 , pp. 1211-1218
    • Bidney, D.L.1    Reeck, G.R.2
  • 17
    • 0018786966 scopus 로고
    • Preferential affinity of high molecular weight high mobility group non-histone chromatin proteins for single-stranded DNA
    • Isackson, P.J., Fishback, J.L., Bidney, D.L., and Reeck, G.R. (1979) Preferential affinity of high molecular weight high mobility group non-histone chromatin proteins for single-stranded DNA. J. Biol. Chem. 254, 5569-5572
    • (1979) J. Biol. Chem. , vol.254 , pp. 5569-5572
    • Isackson, P.J.1    Fishback, J.L.2    Bidney, D.L.3    Reeck, G.R.4
  • 18
    • 0021298143 scopus 로고
    • Unwinding of DNA by nonhistone chromosomal protein HMG(1+2) from pig thymus as determined with endonuclease
    • Yoshida, M. and Shimura, K. (1984) Unwinding of DNA by nonhistone chromosomal protein HMG(1+2) from pig thymus as determined with endonuclease. J. Biochem. 95, 117-124
    • (1984) J. Biochem. , vol.95 , pp. 117-124
    • Yoshida, M.1    Shimura, K.2
  • 19
    • 0022423921 scopus 로고
    • Hierarchy of binding sites for chromosomal proteins HMG1 and 2 in supercoiled deoxyribonucleic acid
    • Hamada, H. and Bustin, M. (1985) Hierarchy of binding sites for chromosomal proteins HMG1 and 2 in supercoiled deoxyribonucleic acid. Biochemistry 24, 1428-1433
    • (1985) Biochemistry , vol.24 , pp. 1428-1433
    • Hamada, H.1    Bustin, M.2
  • 20
    • 0024584528 scopus 로고
    • Specific recognition of cruciform DNA by nuclear protein HMG1
    • Bianchi, M.E., Beltrame, M., and Paonessa, G. (1989) Specific recognition of cruciform DNA by nuclear protein HMG1. Science 243, 1056-1059
    • (1989) Science , vol.243 , pp. 1056-1059
    • Bianchi, M.E.1    Beltrame, M.2    Paonessa, G.3
  • 21
    • 0025201721 scopus 로고
    • Chromosomal protein HMG1 removes the transcriptional block caused by the cruciform in supercoiled DNA
    • Waga, S., Mizuno, S., and Yoshida, M. (1990) Chromosomal protein HMG1 removes the transcriptional block caused by the cruciform in supercoiled DNA. J. Biol. Chem. 265, 19424-19428
    • (1990) J. Biol. Chem. , vol.265 , pp. 19424-19428
    • Waga, S.1    Mizuno, S.2    Yoshida, M.3
  • 22
    • 0023933169 scopus 로고
    • Nonhistone protein HMG1 removes the transcriptional block caused by left-handed Z-form segment in a supercoiled DNA
    • Waga, S., Mizuno, S., and Yoshida, M. (1988) Nonhistone protein HMG1 removes the transcriptional block caused by left-handed Z-form segment in a supercoiled DNA. Biochem. Biophys. Res. Commun. 153, 334-339
    • (1988) Biochem. Biophys. Res. Commun. , vol.153 , pp. 334-339
    • Waga, S.1    Mizuno, S.2    Yoshida, M.3
  • 23
    • 0026569275 scopus 로고
    • Specific binding of chromosomal protein HMG1 to DNA damaged by the anticancer drug cisplatin
    • Pil, P.M. and Lippard, S.J. (1992) Specific binding of chromosomal protein HMG1 to DNA damaged by the anticancer drug cisplatin. Science 256, 234-237
    • (1992) Science , vol.256 , pp. 234-237
    • Pil, P.M.1    Lippard, S.J.2
  • 24
    • 0021381205 scopus 로고
    • 2+-dependent unwinding of DNA by nonhistone chromosomal protein HMG(1+2) from pig thymus as determined by DNA melting temperature analysis
    • 2+-dependent unwinding of DNA by nonhistone chromosomal protein HMG(1+2) from pig thymus as determined by DNA melting temperature analysis. J. Biochem. 95, 423-429
    • (1984) J. Biochem. , vol.95 , pp. 423-429
    • Makiguchi, K.1    Chida, Y.2    Yoshida, M.3    Shimura, K.4
  • 25
    • 0024401923 scopus 로고
    • High mobility group protein 1 preferentially conserves torsion in negatively super-coiled DNA
    • Sheflin, L.G. and Spaulding, S.W. (1989) High mobility group protein 1 preferentially conserves torsion in negatively super-coiled DNA. Biochemistry 28, 5658-5664
    • (1989) Biochemistry , vol.28 , pp. 5658-5664
    • Sheflin, L.G.1    Spaulding, S.W.2
  • 26
    • 0027216519 scopus 로고
    • The nonspecific DNA binding and -bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structure
    • Paull, T.T., Haykinson, M.J., and Johnson, R.C. (1993) The nonspecific DNA binding and -bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structure. Genes Dev. 7, 1521-1534
    • (1993) Genes Dev. , vol.7 , pp. 1521-1534
    • Paull, T.T.1    Haykinson, M.J.2    Johnson, R.C.3
  • 27
    • 0027359690 scopus 로고
    • High-mobility-group 1 protein mediates DNA bending as determined by ring closures
    • Pil, P.M., Chow, C.S., and Lippard, S.J. (1993) High-mobility-group 1 protein mediates DNA bending as determined by ring closures. Proc. Natl. Acad. Sci USA 90, 9465-9469
    • (1993) Proc. Natl. Acad. Sci USA , vol.90 , pp. 9465-9469
    • Pil, P.M.1    Chow, C.S.2    Lippard, S.J.3
  • 30
    • 0029563931 scopus 로고
    • Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronuclear three- and four-dimensional NMR spectroseopy
    • Hardman, C.H., Broadhurst, R.W., Raine, A.R., Grasser, K.D., Thomas, J.O., and Laue, E.D. (1995) Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronuclear three- and four-dimensional NMR spectroseopy. Biochemistry 34, 16596-16607
    • (1995) Biochemistry , vol.34 , pp. 16596-16607
    • Hardman, C.H.1    Broadhurst, R.W.2    Raine, A.R.3    Grasser, K.D.4    Thomas, J.O.5    Laue, E.D.6
  • 31
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F.W. and Moffatt, B.A, (1986) Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189, 113-130
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 32
    • 0025778597 scopus 로고
    • Bipartite functional map of the E. coli RNA polymerase alpha subunit: Involvement of the C-terminal region in transcription activation by cAMP-CRP
    • Igarashi, K. and Iahihama, A. (1991) Bipartite functional map of the E. coli RNA polymerase alpha subunit: involvement of the C-terminal region in transcription activation by cAMP-CRP. Cell 65, 1015-1022
    • (1991) Cell , vol.65 , pp. 1015-1022
    • Igarashi, K.1    Iahihama, A.2
  • 33
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa
    • Schagger, H. and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa. Anal. Biochem. 166, 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 34
    • 0027373797 scopus 로고
    • Lactose represser-operator DNA interactions: Kinetic analysis by a surface plasmon resonance biosensor
    • Bondeson, K., Frostell-Karlsson, A., Fägerstam, L., and Magnusson, G. (1993) Lactose represser-operator DNA interactions: Kinetic analysis by a surface plasmon resonance biosensor. Anal. Biochem. 214, 245-251
    • (1993) Anal. Biochem. , vol.214 , pp. 245-251
    • Bondeson, K.1    Frostell-Karlsson, A.2    Fägerstam, L.3    Magnusson, G.4
  • 35
    • 0028269682 scopus 로고
    • Real-time DNA binding measurements of the ETS1 recombinant oncoproteins reveal significant kinetic differences between the p42 and p51 isoform
    • Fisher, R.J., Fivash, M., Casas-Finet, J., Erickson, J.W., Kondoh, A., Bladen, S.V., Fisher, C., Watson, D.K., and Papas, T. (1994) Real-time DNA binding measurements of the ETS1 recombinant oncoproteins reveal significant kinetic differences between the p42 and p51 isoform. Protein Sci. 3, 257-266
    • (1994) Protein Sci. , vol.3 , pp. 257-266
    • Fisher, R.J.1    Fivash, M.2    Casas-Finet, J.3    Erickson, J.W.4    Kondoh, A.5    Bladen, S.V.6    Fisher, C.7    Watson, D.K.8    Papas, T.9
  • 36
    • 0028963302 scopus 로고
    • Probing the molecular mechanism of action of co-repressor in the E. coli methionine represser-operator complex using surface plasmon resonance (SPR)
    • Parsons, I.D., Persson, B., Mekhalfia, A., Blackburn, G.M., and Stockley, P.G. (1995) Probing the molecular mechanism of action of co-repressor in the E. coli methionine represser-operator complex using surface plasmon resonance (SPR). Nucleic Acids Res. 23, 211-216
    • (1995) Nucleic Acids Res. , vol.23 , pp. 211-216
    • Parsons, I.D.1    Persson, B.2    Mekhalfia, A.3    Blackburn, G.M.4    Stockley, P.G.5
  • 38
    • 0022183264 scopus 로고
    • Nonhistone chromosomal protein HMG1 interaction with DNA
    • Butler, A.P., Mardian, J.K.W., and Olins, D.E. (1985) Nonhistone chromosomal protein HMG1 interaction with DNA. J. Biol. Chem. 260, 10613-10620
    • (1985) J. Biol. Chem. , vol.260 , pp. 10613-10620
    • Butler, A.P.1    Mardian, J.K.W.2    Olins, D.E.3
  • 39
    • 0028080844 scopus 로고
    • Effect of pH on interactions between DNA and high-mobility group protein HMG1
    • Kohlstaedt, L.A. and Cole, R.D. (1994) Effect of pH on interactions between DNA and high-mobility group protein HMG1. Biochemistry 33, 12702-12707
    • (1994) Biochemistry , vol.33 , pp. 12702-12707
    • Kohlstaedt, L.A.1    Cole, R.D.2
  • 40
    • 0027330923 scopus 로고
    • The hLEF/TCF-1a HMG protein contains a context-dependent transcriptional activation domain that induces the TCRα enhancer in T cells
    • Carlsson, P., Waterman, M.L., and Jones, K.A. (1993) The hLEF/TCF-1a HMG protein contains a context-dependent transcriptional activation domain that induces the TCRα enhancer in T cells. Genes Dev. 7, 2418-2430
    • (1993) Genes Dev. , vol.7 , pp. 2418-2430
    • Carlsson, P.1    Waterman, M.L.2    Jones, K.A.3
  • 41
    • 0028937619 scopus 로고
    • Increased DNA-bending activity and higher affinity DNA binding of high mobility group protein HMG-1 prepared without acids
    • Wagner, J.P., Quill, D.M., and Pettijohn, D.E. (1995) Increased DNA-bending activity and higher affinity DNA binding of high mobility group protein HMG-1 prepared without acids. J. Biol. Chem. 270, 7394-7398
    • (1995) J. Biol. Chem. , vol.270 , pp. 7394-7398
    • Wagner, J.P.1    Quill, D.M.2    Pettijohn, D.E.3
  • 42
    • 0030922526 scopus 로고    scopus 로고
    • Nuclear accumulation of HMG2 protein is mediated by basic regions interspaced with a long DNA-binding sequence, and retention within the nucleus requires the acidic carboxyl terminus
    • Shirakawa, H., Tanigawa, T., Sugiyama, S., Kobayashi, M., Terashima, T., Yoshida, K., Arai, T., and Yoshida, M. (1997) Nuclear accumulation of HMG2 protein is mediated by basic regions interspaced with a long DNA-binding sequence, and retention within the nucleus requires the acidic carboxyl terminus. Biochemistry 36, 5992-5999
    • (1997) Biochemistry , vol.36 , pp. 5992-5999
    • Shirakawa, H.1    Tanigawa, T.2    Sugiyama, S.3    Kobayashi, M.4    Terashima, T.5    Yoshida, K.6    Arai, T.7    Yoshida, M.8
  • 43
    • 0030937754 scopus 로고    scopus 로고
    • Linker length and composition influence the flexibility of Oct-1 DNA binding
    • van Leeuven, H.C., Strating, M.J., Rensen, M., de Laat, W., and van del Vliet, P.C. (1997) Linker length and composition influence the flexibility of Oct-1 DNA binding. EMBO J. 16, 2043-2053
    • (1997) EMBO J. , vol.16 , pp. 2043-2053
    • Van Leeuven, H.C.1    Strating, M.J.2    Rensen, M.3    De Laat, W.4    Van Del Vliet, P.C.5
  • 45
    • 0025285226 scopus 로고
    • Primary structure of non-histone chromosomal protein HMG2 revealed by the nucleotide sequence
    • Shirakawa, H., Tsuda, K., and Yoshida, M. (1990) Primary structure of non-histone chromosomal protein HMG2 revealed by the nucleotide sequence. Biochemistry 29, 4419-4423
    • (1990) Biochemistry , vol.29 , pp. 4419-4423
    • Shirakawa, H.1    Tsuda, K.2    Yoshida, M.3
  • 46
    • 0022423480 scopus 로고
    • Isolation and sequence of cDNA clones coding for a member of the family of high mobility group proteins (HMG-T) in trout and analysis of HMG-T-mRNA's in trout tissues
    • Pentecost, B.T., Wright, J.M., and Dixon, G.H. (1985) Isolation and sequence of cDNA clones coding for a member of the family of high mobility group proteins (HMG-T) in trout and analysis of HMG-T-mRNA's in trout tissues. Nucleic Acids Res. 13, 4871-4888
    • (1985) Nucleic Acids Res. , vol.13 , pp. 4871-4888
    • Pentecost, B.T.1    Wright, J.M.2    Dixon, G.H.3
  • 47
  • 48
    • 0028971050 scopus 로고
    • Purification of a high-mobility-group 1 sea-urchin protein and cloning of cDNAs
    • Niemeyer, C.C., Foerster-Ziober, A., and Flytzanis, C.N. (1995) Purification of a high-mobility-group 1 sea-urchin protein and cloning of cDNAs. Gene 164, 211-218
    • (1995) Gene , vol.164 , pp. 211-218
    • Niemeyer, C.C.1    Foerster-Ziober, A.2    Flytzanis, C.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.