메뉴 건너뛰기




Volumn 36, Issue 2, 2004, Pages 186-197

Antigen-binding properties of monoclonal antibodies reactive with human TATA-binding protein and use in immunoaffinity chromatography

Author keywords

Immunoaffinity; mAbs; Monoclonal antibodies; Polyol; TATA binding protein; TBP; Transcription

Indexed keywords

EPITOPE; MONOCLONAL ANTIBODY; RECOMBINANT PROTEIN; TATA BINDING PROTEIN;

EID: 3142533361     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2004.02.020     Document Type: Article
Times cited : (9)

References (45)
  • 1
    • 0038148651 scopus 로고    scopus 로고
    • The genetics of TBP and TBP-related factors
    • Davidson I. The genetics of TBP and TBP-related factors. Trends Biochem. Sci. 28:2003;391-398
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 391-398
    • Davidson, I.1
  • 2
    • 0027268306 scopus 로고
    • TBP, a universal eukaryotic transcription factor
    • Hernandez N. TBP, a universal eukaryotic transcription factor. Genes Dev. 7:1993;1291-1308
    • (1993) Genes Dev. , vol.7 , pp. 1291-1308
    • Hernandez, N.1
  • 3
    • 0028329859 scopus 로고
    • Duality of TBP, the universal transcription factor
    • Struhl K. Duality of TBP, the universal transcription factor. Science. 263:1994;1103-1104
    • (1994) Science , vol.263 , pp. 1103-1104
    • Struhl, K.1
  • 4
    • 0033964073 scopus 로고    scopus 로고
    • TBP-associated factors (TAFIIs): Multiple, selective transcriptional mediators in common complexes
    • Green M.R. TBP-associated factors (TAFIIs): multiple, selective transcriptional mediators in common complexes. Trends Biochem. Sci. 25:2000;59-63
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 59-63
    • Green, M.R.1
  • 5
    • 0034609446 scopus 로고    scopus 로고
    • Control of gene expression through regulation of the TATA-binding protein
    • Pugh B.F. Control of gene expression through regulation of the TATA-binding protein. Gene. 255:2000;1-14
    • (2000) Gene , vol.255 , pp. 1-14
    • Pugh, B.F.1
  • 6
    • 0027483012 scopus 로고
    • Co-crystal structure of TBP recognizing the minor groove of a TATA element
    • Kim J.L., Nikolov D.B., Burley S.K. Co-crystal structure of TBP recognizing the minor groove of a TATA element. Nature. 365:1993;520-527
    • (1993) Nature , vol.365 , pp. 520-527
    • Kim, J.L.1    Nikolov, D.B.2    Burley, S.K.3
  • 7
    • 0027504913 scopus 로고
    • Crystal structure of a yeast TBP/TATA-box complex
    • Kim Y., Geiger J.H., Hahn S., Sigler P.B. Crystal structure of a yeast TBP/TATA-box complex. Nature. 365:1993;512-520
    • (1993) Nature , vol.365 , pp. 512-520
    • Kim, Y.1    Geiger, J.H.2    Hahn, S.3    Sigler, P.B.4
  • 8
    • 0035024076 scopus 로고    scopus 로고
    • Multiple functions of the nonconserved N-terminal domain of yeast TATA-binding protein
    • Lee M., Struhl K. Multiple functions of the nonconserved N-terminal domain of yeast TATA-binding protein. Genetics. 158:2001;87-93
    • (2001) Genetics , vol.158 , pp. 87-93
    • Lee, M.1    Struhl, K.2
  • 9
    • 0029744077 scopus 로고    scopus 로고
    • Analysis of polyglutamine-coding repeats in the TATA-binding protein from different human populations and in patients with schizophrenia and bipolar affective disorder
    • Rubinsztein D.C., Leggo J., Crow T.J., Delisi L.E., Walsh C., Jain S., Paykel E.S. Analysis of polyglutamine-coding repeats in the TATA-binding protein from different human populations and in patients with schizophrenia and bipolar affective disorder. Am. J. Med. Genet. 67:1996;495-498
    • (1996) Am. J. Med. Genet. , vol.67 , pp. 495-498
    • Rubinsztein, D.C.1    Leggo, J.2    Crow, T.J.3    Delisi, L.E.4    Walsh, C.5    Jain, S.6    Paykel, E.S.7
  • 10
    • 0025352364 scopus 로고
    • Highly conserved core domain and unique N terminus with presumptive regulatory motifs in a human TATA factor (TFIID)
    • Hoffman A., Sinn E., Yamamoto T., Wang J., Roy A., Horikoshi M., Roeder R.G. Highly conserved core domain and unique N terminus with presumptive regulatory motifs in a human TATA factor (TFIID). Nature. 346:1990;387-390
    • (1990) Nature , vol.346 , pp. 387-390
    • Hoffman, A.1    Sinn, E.2    Yamamoto, T.3    Wang, J.4    Roy, A.5    Horikoshi, M.6    Roeder, R.G.7
  • 12
    • 0025375345 scopus 로고
    • Functional domains and upstream activation properties of cloned human TATA binding protein
    • Peterson M.G., Tanese N., Pugh B.F., Tjian R. Functional domains and upstream activation properties of cloned human TATA binding protein. Science. 248:1990;1625-1630
    • (1990) Science , vol.248 , pp. 1625-1630
    • Peterson, M.G.1    Tanese, N.2    Pugh, B.F.3    Tjian, R.4
  • 17
    • 0027168221 scopus 로고
    • DNA topology and a minimal set of basal factors for transcription by RNA polymerase II
    • Parvin J.D., Sharp P.A. DNA topology and a minimal set of basal factors for transcription by RNA polymerase II. Cell. 73:1993;533-540
    • (1993) Cell , vol.73 , pp. 533-540
    • Parvin, J.D.1    Sharp, P.A.2
  • 18
    • 0027168947 scopus 로고
    • Identification of a minimal set of proteins that is sufficient for accurate initiation of transcription by RNA polymerase II
    • Tyree C.M., George C.P., Lira-DeVito L.M., Wampler S.L., Dahmus M.E., Zawel L., Kadonaga J.T. Identification of a minimal set of proteins that is sufficient for accurate initiation of transcription by RNA polymerase II. Genes Dev. 7:1993;1254-1265
    • (1993) Genes Dev. , vol.7 , pp. 1254-1265
    • Tyree, C.M.1    George, C.P.2    Lira-Devito, L.M.3    Wampler, S.L.4    Dahmus, M.E.5    Zawel, L.6    Kadonaga, J.T.7
  • 19
    • 0028104678 scopus 로고
    • Initiation of transcription by RNA polymerase II is limited by melting of the promoter DNA in the region immediately upstream of the initiation site
    • Pan G., Greenblatt J. Initiation of transcription by RNA polymerase II is limited by melting of the promoter DNA in the region immediately upstream of the initiation site. J. Biol. Chem. 269:1994;30101-30104
    • (1994) J. Biol. Chem. , vol.269 , pp. 30101-30104
    • Pan, G.1    Greenblatt, J.2
  • 20
    • 0029851428 scopus 로고    scopus 로고
    • Immunoaffinity purification of RNA polymerase II and transcription factors using polyol-responsive monoclonal antibodies
    • Thompson N.E., Burgess R.R. Immunoaffinity purification of RNA polymerase II and transcription factors using polyol-responsive monoclonal antibodies. Methods Enzymol. 274:1996;513-526
    • (1996) Methods Enzymol. , vol.274 , pp. 513-526
    • Thompson, N.E.1    Burgess, R.R.2
  • 21
    • 39749143883 scopus 로고    scopus 로고
    • Identification of polyol-responsive monoclonal antibodies for use in immunoaffinity chromatography
    • Ausubel F.M. et al. New York: Wiley
    • Thompson N.E., Burgess R.R. Identification of polyol-responsive monoclonal antibodies for use in immunoaffinity chromatography. Ausubel F.M., et al. Current Protocols in Molecular Biology. vol. 2:2001;11.18.1-11.18.9 Wiley, New York
    • (2001) Current Protocols in Molecular Biology , vol.2 , pp. 11181-11189
    • Thompson, N.E.1    Burgess, R.R.2
  • 22
    • 0036669677 scopus 로고    scopus 로고
    • Advances in gentle immunoaffinity chromatography
    • Burgess R.R., Thompson N.E. Advances in gentle immunoaffinity chromatography. Curr. Opin. Biotechnol. 13:2002;304-308
    • (2002) Curr. Opin. Biotechnol. , vol.13 , pp. 304-308
    • Burgess, R.R.1    Thompson, N.E.2
  • 23
    • 0026702168 scopus 로고
    • Isolation and characterization of a polyol-responsive monoclonal antibody useful for gentle purification of Escherichia coli RNA polymerase
    • Thompson N.E., Hager D.A., Burgess R.R. Isolation and characterization of a polyol-responsive monoclonal antibody useful for gentle purification of Escherichia coli RNA polymerase. Biochemistry. 31:1992;7003-7008
    • (1992) Biochemistry , vol.31 , pp. 7003-7008
    • Thompson, N.E.1    Hager, D.A.2    Burgess, R.R.3
  • 24
    • 0016748262 scopus 로고
    • A new method for the large-scale purification of wheat germ DNA-dependent RNA polymerase II
    • Jendrisak J.J., Burgess R.R. A new method for the large-scale purification of wheat germ DNA-dependent RNA polymerase II. Biochemistry. 14:1975;4639-4645
    • (1975) Biochemistry , vol.14 , pp. 4639-4645
    • Jendrisak, J.J.1    Burgess, R.R.2
  • 25
    • 0025256911 scopus 로고
    • Purification of eukaryotic RNA polymerase II by immunoaffinity chromatography. Elution of active enzyme with protein stabilizing agents from a polyol-responsive monoclonal antibody
    • Thompson N.E., Aronson D.B., Burgess R.R. Purification of eukaryotic RNA polymerase II by immunoaffinity chromatography. Elution of active enzyme with protein stabilizing agents from a polyol-responsive monoclonal antibody. J. Biol. Chem. 265:1990;7069-7077
    • (1990) J. Biol. Chem. , vol.265 , pp. 7069-7077
    • Thompson, N.E.1    Aronson, D.B.2    Burgess, R.R.3
  • 26
    • 0028518926 scopus 로고
    • Purification of recombinant human transcription factor IIB by immunoaffinity chromatography
    • Thompson N.E., Burgess R.R. Purification of recombinant human transcription factor IIB by immunoaffinity chromatography. Protein Expr. Purif. 5:1994;468-474
    • (1994) Protein Expr. Purif. , vol.5 , pp. 468-474
    • Thompson, N.E.1    Burgess, R.R.2
  • 27
    • 0024328155 scopus 로고
    • Inhibition of in vivo and in vitro transcription by monoclonal antibodies prepared against wheat germ RNA polymerase II that react with the heptapeptide repeat of eukaryotic RNA polymerase II
    • Thompson N.E., Steinberg T.H., Aronson D.B., Burgess R.R. Inhibition of in vivo and in vitro transcription by monoclonal antibodies prepared against wheat germ RNA polymerase II that react with the heptapeptide repeat of eukaryotic RNA polymerase II. J. Biol. Chem. 264:1989;11511-11520
    • (1989) J. Biol. Chem. , vol.264 , pp. 11511-11520
    • Thompson, N.E.1    Steinberg, T.H.2    Aronson, D.B.3    Burgess, R.R.4
  • 28
    • 0003448569 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press. (pp. 139-243)
    • Harlow E., Lane D. Antibodies: A Laboratory Manual. 1988;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. (pp. 139-243)
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 29
    • 0345356399 scopus 로고    scopus 로고
    • Development of an epitope tag for the gentle purification of proteins by immunoaffinity chromatography: Application to epitope-tagged green fluorescent protein
    • Thompson N.E., Arthur T.M., Burgess R.R. Development of an epitope tag for the gentle purification of proteins by immunoaffinity chromatography: application to epitope-tagged green fluorescent protein. Anal. Biochem. 323:2003;171-179
    • (2003) Anal. Biochem. , vol.323 , pp. 171-179
    • Thompson, N.E.1    Arthur, T.M.2    Burgess, R.R.3
  • 30
    • 0023784184 scopus 로고
    • Structure and function of the σ-70 subunit of Escherichia coli RNA polymerase. Monoclonal antibodies: Localization of epitopes by peptide mapping and effects on transcription
    • Strickland M.S., Thompson N.E., Burgess R.R. Structure and function of the σ-70 subunit of Escherichia coli RNA polymerase. Monoclonal antibodies: localization of epitopes by peptide mapping and effects on transcription. Biochemistry. 27:1988;5755-5762
    • (1988) Biochemistry , vol.27 , pp. 5755-5762
    • Strickland, M.S.1    Thompson, N.E.2    Burgess, R.R.3
  • 32
    • 0026667121 scopus 로고
    • Functional binding of the TATA box binding component of transcription factor TFIID to the -30 region of TATA-less promoters
    • Wiley S.R., Kraus R.J., Mertz J.E. Functional binding of the TATA box binding component of transcription factor TFIID to the -30 region of TATA-less promoters. Proc. Natl. Acad. Sci. USA. 89:1992;5814-5818
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5814-5818
    • Wiley, S.R.1    Kraus, R.J.2    Mertz, J.E.3
  • 33
    • 0023732884 scopus 로고
    • Factors involved in specific transcription by mammalian RNA polymerase II: Purification, genetic specificity, and TATA box-promoter interactions of TFIID
    • Nakajima N., Horikoshi M., Roeder R.G. Factors involved in specific transcription by mammalian RNA polymerase II: purification, genetic specificity, and TATA box-promoter interactions of TFIID. Mol. Cell. Biol. 8:1988;4028-4040
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4028-4040
    • Nakajima, N.1    Horikoshi, M.2    Roeder, R.G.3
  • 35
    • 0026480738 scopus 로고
    • A TBP complex essential for transcription from TATA-less but not TATA-containing RNA polymerase III promoters is part of the TFIIIB fraction
    • Lobo S.M., Tanaka M., Sullivan M., Hernandez N. A TBP complex essential for transcription from TATA-less but not TATA-containing RNA polymerase III promoters is part of the TFIIIB fraction. Cell. 71:1992;1029-1040
    • (1992) Cell , vol.71 , pp. 1029-1040
    • Lobo, S.M.1    Tanaka, M.2    Sullivan, M.3    Hernandez, N.4
  • 36
    • 0028178522 scopus 로고
    • The N-terminal domain of the human TATA-binding protein plays a role in transcription from TATA-containing RNA polymerase II and III promoters
    • Lescure A., Lutz Y., Eberhard D., Jacq X., Krol A., Grummt I., Davidson I., Chambon P., Tora L. The N-terminal domain of the human TATA-binding protein plays a role in transcription from TATA-containing RNA polymerase II and III promoters. EMBO J. 13:1994;1166-1175
    • (1994) EMBO J. , vol.13 , pp. 1166-1175
    • Lescure, A.1    Lutz, Y.2    Eberhard, D.3    Jacq, X.4    Krol, A.5    Grummt, I.6    Davidson, I.7    Chambon, P.8    Tora, L.9
  • 37
    • 0029926760 scopus 로고    scopus 로고
    • Monoclonal antibodies directed against the amino-terminal domain of human TBP cross-react with TBP from other species
    • Ruppert S.M.L., McCulloch V., Meyer M., Bautista C., Falkowski M., Stunnenberg H.G., Hernandez N. Monoclonal antibodies directed against the amino-terminal domain of human TBP cross-react with TBP from other species. Hybridoma. 15:1996;55-68
    • (1996) Hybridoma , vol.15 , pp. 55-68
    • Ruppert, S.M.L.1    McCulloch, V.2    Meyer, M.3    Bautista, C.4    Falkowski, M.5    Stunnenberg, H.G.6    Hernandez, N.7
  • 38
    • 0028941547 scopus 로고
    • Identification of cis-acting elements that can obviate a requirement for the C-terminal domain of RNA polymerase II
    • Buermeyer A.B., Strasheim L.A., McMahon S.L., Farnham P.J. Identification of cis-acting elements that can obviate a requirement for the C-terminal domain of RNA polymerase II. J. Biol. Chem. 270:1995;6798-6807
    • (1995) J. Biol. Chem. , vol.270 , pp. 6798-6807
    • Buermeyer, A.B.1    Strasheim, L.A.2    McMahon, S.L.3    Farnham, P.J.4
  • 39
    • 0029130075 scopus 로고
    • Bovine papillomavirus type 1 E2 transcriptional regulators directly bind two cellular transcription factors TFIID and TFIIB
    • Rank N.M., Lambert P.F. Bovine papillomavirus type 1 E2 transcriptional regulators directly bind two cellular transcription factors TFIID and TFIIB. J. Virol. 69:1995;6323-6334
    • (1995) J. Virol. , vol.69 , pp. 6323-6334
    • Rank, N.M.1    Lambert, P.F.2
  • 40
    • 0030058673 scopus 로고    scopus 로고
    • The major transcriptional transactivation domain of simian virus 40 large T antigen associates nonconcurrently with multiple components in the transcriptional preinitiation complex
    • Johnston S.D., Yu X.-M., Mertz J.E. The major transcriptional transactivation domain of simian virus 40 large T antigen associates nonconcurrently with multiple components in the transcriptional preinitiation complex. J. Virol. 70:1996;1191-1202
    • (1996) J. Virol. , vol.70 , pp. 1191-1202
    • Johnston, S.D.1    Yu, X.-M.2    Mertz, J.E.3
  • 41
    • 0029829364 scopus 로고    scopus 로고
    • Mitotic regulation of TFIID: Inhibition of activator-dependent transcription and changes in subcellular localization
    • Segil N., Guermah M., Hoffman A., Roeder R.G., Heintz N. Mitotic regulation of TFIID: inhibition of activator-dependent transcription and changes in subcellular localization. Genes Dev. 10:1996;2389-2400
    • (1996) Genes Dev. , vol.10 , pp. 2389-2400
    • Segil, N.1    Guermah, M.2    Hoffman, A.3    Roeder, R.G.4    Heintz, N.5
  • 42
    • 0033230436 scopus 로고    scopus 로고
    • Immunoaffinity purification of the RAP30 subunit of human transcription factor IIF
    • Thompson N.E., Burgess R.R. Immunoaffinity purification of the RAP30 subunit of human transcription factor IIF. Protein Expr. Purif. 17:1999;260-266
    • (1999) Protein Expr. Purif. , vol.17 , pp. 260-266
    • Thompson, N.E.1    Burgess, R.R.2
  • 44
    • 0029934276 scopus 로고    scopus 로고
    • Rapid purification of the oxygenase component of toluene dioxygenase from a polyol-responsive monoclonal antibody
    • Lynch N.A., Jiang H., Gibson D.T. Rapid purification of the oxygenase component of toluene dioxygenase from a polyol-responsive monoclonal antibody. Appl. Environ. Microbiol. 62:1996;2133-2137
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2133-2137
    • Lynch, N.A.1    Jiang, H.2    Gibson, D.T.3
  • 45
    • 0037039309 scopus 로고    scopus 로고
    • A trithorax-group complex purified from Saccharomyces cerevisiae is required for methylation of histone H3
    • Nagy P.L., Griesenbeck J., Kornberg R.D., Cleary M.L. A trithorax-group complex purified from Saccharomyces cerevisiae is required for methylation of histone H3. Proc. Natl. Acad. Sci. USA. 99:2002;90-94
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 90-94
    • Nagy, P.L.1    Griesenbeck, J.2    Kornberg, R.D.3    Cleary, M.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.