메뉴 건너뛰기




Volumn 377, Issue 1-2, 2006, Pages 33-45

Cloning the genes and DNA binding properties of High Mobility Group B1 (HMGB1) proteins from the human blood flukes Schistosoma mansoni and Schistosoma japonicum

Author keywords

DNA bending; DNA binding; DNA supercoiling; Genomic structure; S. japonicum HMGB1 protein; S. mansoni HMGB1 protein

Indexed keywords

ASPARTIC ACID; CURVED DNA; DNA TOPOISOMERASE; GLUTAMIC ACID; HELMINTH DNA; HIGH MOBILITY GROUP A PROTEIN; HIGH MOBILITY GROUP B PROTEIN; HIGH MOBILITY GROUP B1 PROTEIN; SERINE;

EID: 33746171703     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2006.03.001     Document Type: Article
Times cited : (19)

References (52)
  • 2
    • 0029070956 scopus 로고
    • The HMG-1box protein family: classification and functional relationships
    • Baxevanis A.D., and Landsman D. The HMG-1box protein family: classification and functional relationships. Nucleic Acids Res. 23 (1995) 1604-1613
    • (1995) Nucleic Acids Res. , vol.23 , pp. 1604-1613
    • Baxevanis, A.D.1    Landsman, D.2
  • 3
    • 0024584528 scopus 로고
    • Specific recognition of cruciform DNA by nuclear protein HMG1
    • Bianchi M.E., Beltrame M., and Paonessa G. Specific recognition of cruciform DNA by nuclear protein HMG1. Science 243 (1989) 1056-1059
    • (1989) Science , vol.243 , pp. 1056-1059
    • Bianchi, M.E.1    Beltrame, M.2    Paonessa, G.3
  • 5
    • 4243824006 scopus 로고    scopus 로고
    • The DNA chaperone HMGB1 facilitates ACF/CHRAC-dependent nucleosome sliding
    • Bonaldi Q.T., Langst G., Strohner R., Becker P.B., and Bianchi M.E. The DNA chaperone HMGB1 facilitates ACF/CHRAC-dependent nucleosome sliding. EMBO J. 21 (2002) 6865-6873
    • (2002) EMBO J. , vol.21 , pp. 6865-6873
    • Bonaldi, Q.T.1    Langst, G.2    Strohner, R.3    Becker, P.B.4    Bianchi, M.E.5
  • 6
    • 0032814140 scopus 로고    scopus 로고
    • Regulation of DNA-dependent activities by the functional motifs of the high-mobility-group chromosomal proteins
    • Bustin P.M. Regulation of DNA-dependent activities by the functional motifs of the high-mobility-group chromosomal proteins. Mol. Cell. Biol. 19 (1999) 5237-5246
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5237-5246
    • Bustin, P.M.1
  • 7
    • 0021010763 scopus 로고
    • DNA and histone H1 interact with different domains of HMG 1 and 2 proteins
    • Carballo M., Puigdomenech P., and Palau J. DNA and histone H1 interact with different domains of HMG 1 and 2 proteins. EMBO J. 2 (1983) 1759-1764
    • (1983) EMBO J. , vol.2 , pp. 1759-1764
    • Carballo, M.1    Puigdomenech, P.2    Palau, J.3
  • 10
    • 0028147390 scopus 로고
    • Characterization of a HMG2-like protein from Schistosoma mansoni
    • Fantappié M.R., and Rumjanek F.D. Characterization of a HMG2-like protein from Schistosoma mansoni. Parasitology 108 (1994) 43-50
    • (1994) Parasitology , vol.108 , pp. 43-50
    • Fantappié, M.R.1    Rumjanek, F.D.2
  • 12
    • 0030586235 scopus 로고    scopus 로고
    • The active gene that encodes human high mobility group 1 protein (HMG1) contains introns and maps to chromosome 13
    • Ferrari S., Finelli P., Rocchi M., and Bianchi M.E. The active gene that encodes human high mobility group 1 protein (HMG1) contains introns and maps to chromosome 13. Genomics 35 (1996) 367-371
    • (1996) Genomics , vol.35 , pp. 367-371
    • Ferrari, S.1    Finelli, P.2    Rocchi, M.3    Bianchi, M.E.4
  • 13
    • 30544451614 scopus 로고    scopus 로고
    • Cloning and characterization of a high mobility group box 1 (HMGB1) homologue protein from Schistosoma mansoni
    • Gnanasekar M., Velusamy R., He Y.-X., and Ramaswamy K. Cloning and characterization of a high mobility group box 1 (HMGB1) homologue protein from Schistosoma mansoni. Mol. Biochem. Parasitol. 145 (2006) 137-146
    • (2006) Mol. Biochem. Parasitol. , vol.145 , pp. 137-146
    • Gnanasekar, M.1    Velusamy, R.2    He, Y.-X.3    Ramaswamy, K.4
  • 14
    • 0017366660 scopus 로고
    • The isolation and purification of the high mobility group (HMG) nonhistone chromosomal proteins
    • Goodwin G.H., and Johns E.W. The isolation and purification of the high mobility group (HMG) nonhistone chromosomal proteins. Methods Cell Biol. 16 (1977) 257-267
    • (1977) Methods Cell Biol. , vol.16 , pp. 257-267
    • Goodwin, G.H.1    Johns, E.W.2
  • 15
    • 0346669751 scopus 로고    scopus 로고
    • Chromatin-associated HMGA and HMGB proteins: versatile co-regulators of DNA-dependent processes
    • Grasser K.D. Chromatin-associated HMGA and HMGB proteins: versatile co-regulators of DNA-dependent processes. Plant Mol. Biol. 53 (2003) 281-295
    • (2003) Plant Mol. Biol. , vol.53 , pp. 281-295
    • Grasser, K.D.1
  • 16
    • 0032079906 scopus 로고    scopus 로고
    • DNA-binding properties of the tandem HMG boxes of high-mobility-group protein 1 (HMG1)
    • Grasser K.D., et al. DNA-binding properties of the tandem HMG boxes of high-mobility-group protein 1 (HMG1). Eur. J. Biochem. 253 (1998) 787-795
    • (1998) Eur. J. Biochem. , vol.253 , pp. 787-795
    • Grasser, K.D.1
  • 17
    • 0035823644 scopus 로고    scopus 로고
    • Elevated serum levels of TNF-alpha, sTNF-RI and sTNF-RII in murine schistosomias correlate with schistosome oviposition and circumoval granuloma formation
    • Haseeb M.A., Shirazian D.J., and Preis J. Elevated serum levels of TNF-alpha, sTNF-RI and sTNF-RII in murine schistosomias correlate with schistosome oviposition and circumoval granuloma formation. Cytokine 15 (2001) 266-269
    • (2001) Cytokine , vol.15 , pp. 266-269
    • Haseeb, M.A.1    Shirazian, D.J.2    Preis, J.3
  • 18
    • 0033562334 scopus 로고    scopus 로고
    • Directional binding of HMG-I(Y) on four-way junction DNA and the molecular basis for competitive binding with HMG-1 and histone H1
    • Hill D.A., Pedulla M.L., and Reeves R. Directional binding of HMG-I(Y) on four-way junction DNA and the molecular basis for competitive binding with HMG-1 and histone H1. Nucleic Acids Res. 27 (1999) 2135-2144
    • (1999) Nucleic Acids Res. , vol.27 , pp. 2135-2144
    • Hill, D.A.1    Pedulla, M.L.2    Reeves, R.3
  • 19
    • 4644335083 scopus 로고    scopus 로고
    • 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
    • Knapp S., Muller S., Digilio G., Bonaldi T., Bianchi M.E., and Musco G. 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 (2004) 11992-11997
    • (2004) Biochemistry , vol.43 , pp. 11992-11997
    • Knapp, S.1    Muller, S.2    Digilio, G.3    Bonaldi, T.4    Bianchi, M.E.5    Musco, G.6
  • 20
    • 0028117324 scopus 로고
    • Specific interaction between H1 histone and high mobility protein HMG1
    • Kohlstaedt L.A., and Cole R.D. Specific interaction between H1 histone and high mobility protein HMG1. Biochemistry 33 (1994) 570-775
    • (1994) Biochemistry , vol.33 , pp. 570-775
    • Kohlstaedt, L.A.1    Cole, R.D.2
  • 21
    • 0034711421 scopus 로고    scopus 로고
    • The effect of the acidic tail on the DNA-binding properties of the HMG1,2 class of proteins: insights from tail switching and tail removal
    • Lee K.B., and Thomas J.O. The effect of the acidic tail on the DNA-binding properties of the HMG1,2 class of proteins: insights from tail switching and tail removal. J. Mol. Biol. 30 (2000) 135-149
    • (2000) J. Mol. Biol. , vol.30 , pp. 135-149
    • Lee, K.B.1    Thomas, J.O.2
  • 22
    • 17144376810 scopus 로고    scopus 로고
    • High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal
    • Lotze M.T., and Tracey K.J. High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal. Nat. Rev., Immunol. 5 (2005) 331-342
    • (2005) Nat. Rev., Immunol. , vol.5 , pp. 331-342
    • Lotze, M.T.1    Tracey, K.J.2
  • 23
    • 19444364848 scopus 로고    scopus 로고
    • Helminth genome projects: all or nothing
    • Lukeš J., Horák A., and Scholz T. Helminth genome projects: all or nothing. Trends Parasitol. 21 (2005) 265-266
    • (2005) Trends Parasitol. , vol.21 , pp. 265-266
    • Lukeš, J.1    Horák, A.2    Scholz, T.3
  • 24
    • 1842785761 scopus 로고    scopus 로고
    • A vaccine against Asian schistosomiasis
    • McManus D.P., and Bartley P.B. A vaccine against Asian schistosomiasis. Parasitol. Int. 53 (2004) 163-173
    • (2004) Parasitol. Int. , vol.53 , pp. 163-173
    • McManus, D.P.1    Bartley, P.B.2
  • 26
    • 0033485515 scopus 로고    scopus 로고
    • The structure of a chromosomal high mobility group protein-DNA complex reveals sequence-neutral mechanisms important for non-sequence-specific DNA recognition
    • Murphy IV F.V., Sweet R.M., and Churchill M.E. The structure of a chromosomal high mobility group protein-DNA complex reveals sequence-neutral mechanisms important for non-sequence-specific DNA recognition. EMBO J. 18 (1999) 6610-6618
    • (1999) EMBO J. , vol.18 , pp. 6610-6618
    • Murphy IV, F.V.1    Sweet, R.M.2    Churchill, M.E.3
  • 27
    • 0027216519 scopus 로고
    • The nonspecific DNA binding and - bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structures
    • Paull T.T., Haykinson M.J., and Johnson R.C. The nonspecific DNA binding and - bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structures. Genes Dev. 7 (1993) 1521-1534
    • (1993) Genes Dev. , vol.7 , pp. 1521-1534
    • Paull, T.T.1    Haykinson, M.J.2    Johnson, R.C.3
  • 28
    • 0031566959 scopus 로고    scopus 로고
    • The acidic tail of the high mobility group protein HMG-D modulates the structural selectivity of DNA binding
    • Payet D., and Travers A. The acidic tail of the high mobility group protein HMG-D modulates the structural selectivity of DNA binding. J. Mol. Biol. 266 (1997) 66-75
    • (1997) J. Mol. Biol. , vol.266 , pp. 66-75
    • Payet, D.1    Travers, A.2
  • 29
    • 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. High-mobility-group 1 protein mediates DNA bending as determined by ring closures. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 9465-9469
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 9465-9469
    • Pil, P.M.1    Chow, C.S.2    Lippard, S.J.3
  • 30
    • 0041092343 scopus 로고    scopus 로고
    • HMG box proteins bind to four-way DNA junctions in their open conformation
    • Pöhler J.R., Norman D.G., Bramham J., Bianchi M.E., and Lilley D.M. HMG box proteins bind to four-way DNA junctions in their open conformation. EMBO J. 17 (1998) 817-826
    • (1998) EMBO J. , vol.17 , pp. 817-826
    • Pöhler, J.R.1    Norman, D.G.2    Bramham, J.3    Bianchi, M.E.4    Lilley, D.M.5
  • 31
    • 0026684228 scopus 로고
    • Extraction and partial characterization of non-histone nuclear proteins of Schistosoma mansoni
    • Rabelo E.M., Campos E.G., Fantappié M.R., and Rumjanek F.D. Extraction and partial characterization of non-histone nuclear proteins of Schistosoma mansoni. J. Cell. Biochem. 49 (1992) 172-180
    • (1992) J. Cell. Biochem. , vol.49 , pp. 172-180
    • Rabelo, E.M.1    Campos, E.G.2    Fantappié, M.R.3    Rumjanek, F.D.4
  • 32
    • 0024401923 scopus 로고
    • High mobility group protein 1 preferentially conserves torsion in negatively supercoiled DNA
    • Sheflin L.G., and Spaulding S.W. High mobility group protein 1 preferentially conserves torsion in negatively supercoiled DNA. Biochemistry 28 (1989) 5658-5664
    • (1989) Biochemistry , vol.28 , pp. 5658-5664
    • Sheflin, L.G.1    Spaulding, S.W.2
  • 33
    • 0027156630 scopus 로고
    • The specific interactions of HMG 1 and 2 with negatively supercoiled DNA are modulated by their acidic C-terminal domains and involve cysteine residues in their HMG 1/2 boxes
    • Sheflin L.G., Fucile N.W., and Spaulding S.W. The specific interactions of HMG 1 and 2 with negatively supercoiled DNA are modulated by their acidic C-terminal domains and involve cysteine residues in their HMG 1/2 boxes. Biochemistry 32 (1993) 3238-3248
    • (1993) Biochemistry , vol.32 , pp. 3238-3248
    • Sheflin, L.G.1    Fucile, N.W.2    Spaulding, S.W.3
  • 34
    • 0032562599 scopus 로고    scopus 로고
    • DNA bending by the chromosomal protein HMG1 and its high mobility group box domains. Effect of flanking sequences
    • Štros M. DNA bending by the chromosomal protein HMG1 and its high mobility group box domains. Effect of flanking sequences. J. Biol. Chem. 273 (1998) 10355-10361
    • (1998) J. Biol. Chem. , vol.273 , pp. 10355-10361
    • Štros, M.1
  • 35
    • 0035901480 scopus 로고    scopus 로고
    • Two mutations of basic residues within the N-terminus of HMG1-B domain with different effects on DNA supercoiling and binding to bent DNA
    • Štros M. Two mutations of basic residues within the N-terminus of HMG1-B domain with different effects on DNA supercoiling and binding to bent DNA. Biochemistry 40 (2001) 4769-4779
    • (2001) Biochemistry , vol.40 , pp. 4769-4779
    • Štros, M.1
  • 36
    • 0034680871 scopus 로고    scopus 로고
    • A role of basic residues and the putative intercalating phenylalanine of the HMG-1 box B in DNA supercoiling and binding to four-way DNA junctions
    • Štros M., and Muselíková E. A role of basic residues and the putative intercalating phenylalanine of the HMG-1 box B in DNA supercoiling and binding to four-way DNA junctions. J. Biol. Chem. 275 (2000) 35699-35707
    • (2000) J. Biol. Chem. , vol.275 , pp. 35699-35707
    • Štros, M.1    Muselíková, E.2
  • 37
    • 0032518462 scopus 로고    scopus 로고
    • Formation of large nucleoprotein complexes upon binding of the high-mobility-group (HMG) box B-domain of HMG1 protein to supercoiled DNA
    • Štros M., and Reich J. Formation of large nucleoprotein complexes upon binding of the high-mobility-group (HMG) box B-domain of HMG1 protein to supercoiled DNA. Eur. J. Biochem. 251 (1998) 427-434
    • (1998) Eur. J. Biochem. , vol.251 , pp. 427-434
    • Štros, M.1    Reich, J.2
  • 38
    • 0025119921 scopus 로고
    • 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
    • Štros M., and Vorlíčková M. 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 (1990) 282-288
    • (1990) Int. J. Biol. Macromol. , vol.12 , pp. 282-288
    • Štros, M.1    Vorlíčková, M.2
  • 39
    • 0025127937 scopus 로고
    • Calcium modulates the binding of high-mobility-group protein 1 to DNA
    • Štros M., Bernuès J., and Querol E. Calcium modulates the binding of high-mobility-group protein 1 to DNA. Biochem. Int. 21 (1990) 891-899
    • (1990) Biochem. Int. , vol.21 , pp. 891-899
    • Štros, M.1    Bernuès, J.2    Querol, E.3
  • 40
    • 0028359704 scopus 로고
    • DNA looping by the HMG-box domains of HMG1 and modulation of DNA binding by the acidic C-terminal domain
    • Štros M., Štokrová J., and Thomas J.O. DNA looping by the HMG-box domains of HMG1 and modulation of DNA binding by the acidic C-terminal domain. Nucleic Acids Res. 22 (1994) 1044-1051
    • (1994) Nucleic Acids Res. , vol.22 , pp. 1044-1051
    • Štros, M.1    Štokrová, J.2    Thomas, J.O.3
  • 41
    • 0033944776 scopus 로고    scopus 로고
    • HMG1 protein stimulates DNA end joining by promoting association of DNA molecules via their ends
    • Štros M., Cherny D., and Jovin T.M. HMG1 protein stimulates DNA end joining by promoting association of DNA molecules via their ends. Eur. J. Biochem. 267 (2000) 4088-4097
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4088-4097
    • Štros, M.1    Cherny, D.2    Jovin, T.M.3
  • 42
    • 2642553083 scopus 로고    scopus 로고
    • High-affinity binding of tumor-suppressor protein p53 and HMGB1 to hemicatenated DNA loops
    • Štros M., Muselíková-Polanská E., Pospíšilová Š., and Strauss F. High-affinity binding of tumor-suppressor protein p53 and HMGB1 to hemicatenated DNA loops. Biochemistry 43 (2004) 7215-7225
    • (2004) Biochemistry , vol.43 , pp. 7215-7225
    • Štros, M.1    Muselíková-Polanská, E.2    Pospíšilová, Š.3    Strauss, F.4
  • 43
    • 0034682315 scopus 로고    scopus 로고
    • Blockade of RAGE-amphoterin signalling suppresses tumour growth and metastases
    • Taguchi A., et al. Blockade of RAGE-amphoterin signalling suppresses tumour growth and metastases. Nature 405 (2000) 354-360
    • (2000) Nature , vol.405 , pp. 354-360
    • Taguchi, A.1
  • 44
    • 0028999513 scopus 로고
    • Differences in the DNA-binding properties of the HMG-box domains of HMG1 and the sex-determining factor SRY
    • Teo S.H., Grasser K.D., and Thomas J.O. Differences in the DNA-binding properties of the HMG-box domains of HMG1 and the sex-determining factor SRY. Eur. J. Biochem. 230 (1995) 943-950
    • (1995) Eur. J. Biochem. , vol.230 , pp. 943-950
    • Teo, S.H.1    Grasser, K.D.2    Thomas, J.O.3
  • 45
    • 0035281548 scopus 로고    scopus 로고
    • HMG1 and 2, and related 'architectural' DNA-binding proteins
    • Thomas J.O., and Travers A.A. HMG1 and 2, and related 'architectural' DNA-binding proteins. Trends Biochem. Sci. 26 (2001) 167-174
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 167-174
    • Thomas, J.O.1    Travers, A.A.2
  • 46
    • 0033982040 scopus 로고    scopus 로고
    • Recognition of distorted DNA structures by HMG domains
    • Travers A. Recognition of distorted DNA structures by HMG domains. Curr. Opin. Struct. Biol. 10 (2000) 102-109
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 102-109
    • Travers, A.1
  • 47
    • 0037295617 scopus 로고    scopus 로고
    • Priming the nucleosome: a role for HMGB proteins?
    • Travers R.A.A. Priming the nucleosome: a role for HMGB proteins?. EMBO Rep. 4 (2003) 131-136
    • (2003) EMBO Rep. , vol.4 , pp. 131-136
    • Travers, R.A.A.1
  • 48
    • 3342939967 scopus 로고    scopus 로고
    • Acidic C-tail of HMGB1 is required for its target binding to nucleosome linker DNA and transcription stimulation
    • Ueda T., Chou H., Kawase T., Shirakawa H., and Yoshida M. Acidic C-tail of HMGB1 is required for its target binding to nucleosome linker DNA and transcription stimulation. Biochemistry 43 (2004) 9901-9908
    • (2004) Biochemistry , vol.43 , pp. 9901-9908
    • Ueda, T.1    Chou, H.2    Kawase, T.3    Shirakawa, H.4    Yoshida, M.5
  • 49
    • 0141507054 scopus 로고    scopus 로고
    • Transcriptome analysis of the acoelomate human parasite Schistosoma mansoni
    • Verjovski-Almeida S., et al. Transcriptome analysis of the acoelomate human parasite Schistosoma mansoni. Nat. Genet. 35 2 (2003) 148-157
    • (2003) Nat. Genet. , vol.35 , Issue.2 , pp. 148-157
    • Verjovski-Almeida, S.1
  • 51
    • 0033538467 scopus 로고    scopus 로고
    • HMG-1 as a late mediator of endotoxin lethality in mice
    • Wang H., et al. HMG-1 as a late mediator of endotoxin lethality in mice. Science 285 (1999) 248-251
    • (1999) Science , vol.285 , pp. 248-251
    • Wang, H.1
  • 52
    • 0032548929 scopus 로고    scopus 로고
    • Determinants of DNA binding and bending by the Saccharomyces cerevisiae high mobility group protein NHP6A that are important for its biological activities. Role of the unique N terminus and putative intercalating methionine
    • Yen Y.M., Wong B., and Johnson R.C. Determinants of DNA binding and bending by the Saccharomyces cerevisiae high mobility group protein NHP6A that are important for its biological activities. Role of the unique N terminus and putative intercalating methionine. J. Biol. Chem. 273 (1998) 4424-4435
    • (1998) J. Biol. Chem. , vol.273 , pp. 4424-4435
    • Yen, Y.M.1    Wong, B.2    Johnson, R.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.