메뉴 건너뛰기




Volumn 288, Issue 36, 2013, Pages 26220-26234

Bpur, the lyme disease spirochete's PUR domain protein: Identification as a transcriptional modulator and characterization of nucleic acid interactions

Author keywords

[No Author keywords available]

Indexed keywords

BORRELIA BURGDORFERI; LYME DISEASE; PROTEIN EXPRESSIONS; PROTEIN PRODUCTION; REGULATORY FACTORS; TRANSCRIPTIONAL REPRESSORS;

EID: 84883728097     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.491357     Document Type: Article
Times cited : (24)

References (85)
  • 1
    • 84855900042 scopus 로고    scopus 로고
    • Of ticks, mice and men: Understanding the dual-host lifestyle of Lyme disease spirochaetes
    • Radolf, J. D., Caimano, M. J., Stevenson, B., and Hu, L. T. (2012) Of ticks, mice and men: understanding the dual-host lifestyle of Lyme disease spirochaetes. Nat. Rev. Microbiol. 10, 87-99
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 87-99
    • Radolf, J.D.1    Caimano, M.J.2    Stevenson, B.3    Hu, L.T.4
  • 2
    • 0345714742 scopus 로고    scopus 로고
    • Temporal analysis of Borrelia burgdorferi Erp protein expression throughout the mammal-tick infectious cycle
    • Miller, J. C., von Lackum, K., Babb, K., McAlister, J. D., and Stevenson, B. (2003) Temporal analysis of Borrelia burgdorferi Erp protein expression throughout the mammal-tick infectious cycle. Infect. Immun. 71, 6943-6952
    • (2003) Infect. Immun. , vol.71 , pp. 6943-6952
    • Miller, J.C.1    Von Lackum, K.2    Babb, K.3    McAlister, J.D.4    Stevenson, B.5
  • 4
    • 0034802110 scopus 로고    scopus 로고
    • Analysis of Borrelia burgdorferi gene expression during life cycle phases of the tick vector Ixodes scapularis
    • Gilmore, R. D., Jr., Mbow, M. L., and Stevenson, B. (2001) Analysis of Borrelia burgdorferi gene expression during life cycle phases of the tick vector Ixodes scapularis. Microbes Infect. 3, 799-808
    • (2001) Microbes Infect. , vol.3 , pp. 799-808
    • Gilmore Jr., R.D.1    Mbow, M.L.2    Stevenson, B.3
  • 6
    • 79953327324 scopus 로고    scopus 로고
    • The OspE-related proteins inhibit complement deposition and enhance serum resistance of Borrelia burgdorferi, the lyme disease spirochete
    • Kenedy, M. R., and Akins, D. R. (2011) The OspE-related proteins inhibit complement deposition and enhance serum resistance of Borrelia burgdorferi, the lyme disease spirochete. Infect. Immun. 79, 1451-1457
    • (2011) Infect. Immun. , vol.79 , pp. 1451-1457
    • Kenedy, M.R.1    Akins, D.R.2
  • 7
    • 64049098188 scopus 로고    scopus 로고
    • The Borrelia burgdorferi outer-surface protein ErpX binds mammalian laminin
    • Brissette, C. A., Verma, A., Bowman, A., Cooley, A. E., and Stevenson, B. (2009) The Borrelia burgdorferi outer-surface protein ErpX binds mammalian laminin. Microbiology 155, 863-872
    • (2009) Microbiology , vol.155 , pp. 863-872
    • Brissette, C.A.1    Verma, A.2    Bowman, A.3    Cooley, A.E.4    Stevenson, B.5
  • 9
    • 0036784619 scopus 로고    scopus 로고
    • Complement inhibitor factor H binding to Lyme disease spirochetes is mediated by inducible expression of multiple plasmid-encoded outer surface protein e paralogs
    • Alitalo, A., Meri, T., Lankinen, H., Seppälä, I., Lahdenne, P., Hefty, P. S., Akins, D., and Meri, S. (2002) Complement inhibitor factor H binding to Lyme disease spirochetes is mediated by inducible expression of multiple plasmid-encoded outer surface protein E paralogs. J. Immunol. 169, 3847-3853
    • (2002) J. Immunol. , vol.169 , pp. 3847-3853
    • Alitalo, A.1    Meri, T.2    Lankinen, H.3    Seppälä, I.4    Lahdenne, P.5    Hefty, P.S.6    Akins, D.7    Meri, S.8
  • 10
    • 0036156137 scopus 로고    scopus 로고
    • Differential binding of host complement inhibitor factor H by Borrelia burgdorferi Erp surface proteins: A possible mechanism underlying the expansive host range of Lyme disease spirochetes
    • Stevenson, B., El-Hage, N., Hines, M. A., Miller, J. C., and Babb, K. (2002) Differential binding of host complement inhibitor factor H by Borrelia burgdorferi Erp surface proteins: a possible mechanism underlying the expansive host range of Lyme disease spirochetes. Infect. Immun. 70, 491-497
    • (2002) Infect. Immun. , vol.70 , pp. 491-497
    • Stevenson, B.1    El-Hage, N.2    Hines, M.A.3    Miller, J.C.4    Babb, K.5
  • 11
    • 34548694325 scopus 로고    scopus 로고
    • Borrelia burgdorferi adhesins identified using in vivo phage display
    • Antonara, S., Chafel, R. M., LaFrance, M., and Coburn, J. (2007) Borrelia burgdorferi adhesins identified using in vivo phage display. Mol. Microbiol. 66, 262-276
    • (2007) Mol. Microbiol. , vol.66 , pp. 262-276
    • Antonara, S.1    Chafel, R.M.2    Lafrance, M.3    Coburn, J.4
  • 12
    • 33644780179 scopus 로고    scopus 로고
    • Selective binding of Borrelia burgdorferi OspE paralogs to factor H and serum proteins from diverse animals: Possible expansion of the role of OspE in Lyme disease pathogenesis
    • Hovis, K. M., Tran, E., Sundy, C. M., Buckles, E., McDowell, J. V., and Marconi, R. T. (2006) Selective binding of Borrelia burgdorferi OspE paralogs to factor H and serum proteins from diverse animals: possible expansion of the role of OspE in Lyme disease pathogenesis. Infect. Immun. 74, 1967-1972
    • (2006) Infect. Immun. , vol.74 , pp. 1967-1972
    • Hovis, K.M.1    Tran, E.2    Sundy, C.M.3    Buckles, E.4    McDowell, J.V.5    Marconi, R.T.6
  • 13
    • 0037512362 scopus 로고    scopus 로고
    • Analysis of the OspE determinants involved in binding of factor H and OspE-targeting antibodies elicited during Borrelia burgdorferi infection in mice
    • Metts, M. S., McDowell, J. V., Theisen, M., Hansen, P. R., and Marconi, R. T. (2003) Analysis of the OspE determinants involved in binding of factor H and OspE-targeting antibodies elicited during Borrelia burgdorferi infection in mice. Infect. Immun. 71, 3587-3596
    • (2003) Infect. Immun. , vol.71 , pp. 3587-3596
    • Metts, M.S.1    McDowell, J.V.2    Theisen, M.3    Hansen, P.R.4    Marconi, R.T.5
  • 14
    • 1942539716 scopus 로고    scopus 로고
    • Molecular characterization of Borrelia burgdorferi erp promoter/operator elements
    • Babb, K., McAlister, J. D., Miller, J. C., and Stevenson, B. (2004) Molecular characterization of Borrelia burgdorferi erp promoter/operator elements. J. Bacteriol. 186, 2745-2756
    • (2004) J. Bacteriol. , vol.186 , pp. 2745-2756
    • Babb, K.1    McAlister, J.D.2    Miller, J.C.3    Stevenson, B.4
  • 15
    • 84879826158 scopus 로고    scopus 로고
    • Distribution of cp32 prophages among Lyme disease-causing spirochetes and natural diversity of their lipoprotein-encoding erp Loci
    • Brisson, D., Zhou, W., Jutras, B. L., Casjens, S., and Stevenson, B. (2013) Distribution of cp32 prophages among Lyme disease-causing spirochetes and natural diversity of their lipoprotein-encoding erp Loci. Appl. Environ. Microbiol. 79, 4115-4128
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 4115-4128
    • Brisson, D.1    Zhou, W.2    Jutras, B.L.3    Casjens, S.4    Stevenson, B.5
  • 16
    • 33744989020 scopus 로고    scopus 로고
    • Borrelia burgdorferi EbfC, a novel, chromosomally encoded protein, binds specific DNA sequences adjacent to erp loci on the spirochete's resident cp32 prophages
    • Babb, K., Bykowski, T., Riley, S. P., Miller, M. C., Demoll, E., and Stevenson, B. (2006) Borrelia burgdorferi EbfC, a novel, chromosomally encoded protein, binds specific DNA sequences adjacent to erp loci on the spirochete's resident cp32 prophages. J. Bacteriol. 188, 4331-4339
    • (2006) J. Bacteriol. , vol.188 , pp. 4331-4339
    • Babb, K.1    Bykowski, T.2    Riley, S.P.3    Miller, M.C.4    Demoll, E.5    Stevenson, B.6
  • 19
    • 84866316666 scopus 로고    scopus 로고
    • Borrelia burgdorferi cp32 BpaB modulates expression of the prophage NucP nuclease and SsbP singlestranded DNA-binding protein
    • Chenail, A. M., Jutras, B. L., Adams, C. A., Burns, L. H., Bowman, A., Verma, A., and Stevenson, B. (2012) Borrelia burgdorferi cp32 BpaB modulates expression of the prophage NucP nuclease and SsbP singlestranded DNA-binding protein. J. Bacteriol. 194, 4570-4578
    • (2012) J. Bacteriol. , vol.194 , pp. 4570-4578
    • Chenail, A.M.1    Jutras, B.L.2    Adams, C.A.3    Burns, L.H.4    Bowman, A.5    Verma, A.6    Stevenson, B.7
  • 21
    • 84864014078 scopus 로고    scopus 로고
    • EbfC (YbaB) is a new type of bacterial nucleoid-associated protein and a global regulator of gene expression in the Lyme disease spirochete
    • Jutras, B. L., Bowman, A., Brissette, C. A., Adams, C. A., Verma, A., Chenail, A. M., and Stevenson, B. (2012) EbfC (YbaB) is a new type of bacterial nucleoid-associated protein and a global regulator of gene expression in the Lyme disease spirochete. J. Bacteriol. 194, 3395-3406
    • (2012) J. Bacteriol. , vol.194 , pp. 3395-3406
    • Jutras, B.L.1    Bowman, A.2    Brissette, C.A.3    Adams, C.A.4    Verma, A.5    Chenail, A.M.6    Stevenson, B.7
  • 22
    • 78149492329 scopus 로고    scopus 로고
    • Of bits and bugs-on the use of bioinformatics and a bacterial crystal structure to solve a eukaryotic repeat-protein structure
    • Graebsch, A., Roche, S., Kostrewa, D., Söding, J., and Niessing, D. (2010) Of bits and bugs-on the use of bioinformatics and a bacterial crystal structure to solve a eukaryotic repeat-protein structure. PLoS One 5, e13402
    • (2010) PLoS One , vol.5
    • Graebsch, A.1    Roche, S.2    Kostrewa, D.3    Söding, J.4    Niessing, D.5
  • 23
    • 73249115808 scopus 로고    scopus 로고
    • X-ray structure of Pur reveals a Whirly-like fold and an unusual nucleic-acid binding surface
    • Graebsch, A., Roche, S., and Niessing, D. (2009) X-ray structure of Pur reveals a Whirly-like fold and an unusual nucleic-acid binding surface. Proc. Natl. Acad. Sci. U.S.A. 106, 18521-18526
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 18521-18526
    • Graebsch, A.1    Roche, S.2    Niessing, D.3
  • 24
    • 0242581729 scopus 로고    scopus 로고
    • Single-stranded DNA-binding proteins PUR and PUR bind to a purine-rich negative regulatory element of the-myosin heavy chain gene and control transcriptional and translational regulation of the gene expression Implications in the repression of -myosin heavy chain during heart failure
    • Gupta, M., Sueblinvong, V., Raman, J., Jeevanandam, V., and Gupta, M. P. (2003) Single-stranded DNA-binding proteins PUR and PUR bind to a purine-rich negative regulatory element of the-myosin heavy chain gene and control transcriptional and translational regulation of the gene expression. Implications in the repression of -myosin heavy chain during heart failure. J. Biol. Chem. 278, 44935-44948
    • (2003) J. Biol. Chem. , vol.278 , pp. 44935-44948
    • Gupta, M.1    Sueblinvong, V.2    Raman, J.3    Jeevanandam, V.4    Gupta, M.P.5
  • 26
    • 34547681603 scopus 로고    scopus 로고
    • Pur binds to rCGG repeats and modulates repeat-mediated neurodegeneration in a Drosophila model of fragile X tremor/ataxia syndrome
    • Jin, P., Duan, R., Qurashi, A., Qin, Y., Tian, D., Rosser, T. C., Liu, H., Feng, Y., and Warren, S. T. (2007) Pur binds to rCGG repeats and modulates repeat-mediated neurodegeneration in a Drosophila model of fragile X tremor/ataxia syndrome. Neuron 55, 556-564
    • (2007) Neuron , vol.55 , pp. 556-564
    • Jin, P.1    Duan, R.2    Qurashi, A.3    Qin, Y.4    Tian, D.5    Rosser, T.C.6    Liu, H.7    Feng, Y.8    Warren, S.T.9
  • 29
    • 65549155204 scopus 로고    scopus 로고
    • Purine-rich element binding protein (PUR) induces endoplasmic reticulum stress response, and cell differentiation pathways in prostate cancer cells
    • Inoue, T., Maeno, A., Talbot, C., Jr., Zeng, Y., Yeater, D. B., Leman, E. S., Kulkarni, P., Ogawa, O., and Getzenberg, R. H. (2009) Purine-rich element binding protein (PUR) induces endoplasmic reticulum stress response, and cell differentiation pathways in prostate cancer cells. Prostate 69, 861-873
    • (2009) Prostate , vol.69 , pp. 861-873
    • Inoue, T.1    Maeno, A.2    Talbot Jr., C.3    Zeng, Y.4    Yeater, D.B.5    Leman, E.S.6    Kulkarni, P.7    Ogawa, O.8    Getzenberg, R.H.9
  • 30
    • 0028799664 scopus 로고
    • Cooperative action of cellular proteins YB-1 and Pur with the tumor antigen of the human JC polyomavirus determines their interaction with the viral lytic control element
    • Chen, N. N., Chang, C. F., Gallia, G. L., Kerr, D. A., Johnson, E. M., Krachmarov, C. P., Barr, S. M., Frisque, R. J., Bollag, B., and Khalili, K. (1995) Cooperative action of cellular proteins YB-1 and Pur with the tumor antigen of the human JC polyomavirus determines their interaction with the viral lytic control element. Proc. Natl. Acad. Sci. U.S.A. 92, 1087-1091
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 1087-1091
    • Chen, N.N.1    Chang, C.F.2    Gallia, G.L.3    Kerr, D.A.4    Johnson, E.M.5    Krachmarov, C.P.6    Barr, S.M.7    Frisque, R.J.8    Bollag, B.9    Khalili, K.10
  • 32
    • 78049488129 scopus 로고    scopus 로고
    • Regulation of PURA gene transcription by three promoters generating distinctly spliced 5-prime leaders: A novel means of fine control over tissue specificity and viral signals
    • Wortman, M. J., Hanson, L. K., Martínez-Sobrido, L., Campbell, A. E., Nance, J. A., García-Sastre, A., and Johnson, E. M. (2010) Regulation of PURA gene transcription by three promoters generating distinctly spliced 5-prime leaders: a novel means of fine control over tissue specificity and viral signals. BMC Mol. Biol. 11, 81-96
    • (2010) BMC Mol. Biol. , vol.11 , pp. 81-96
    • Wortman, M.J.1    Hanson, L.K.2    Martínez-Sobrido, L.3    Campbell, A.E.4    Nance, J.A.5    García-Sastre, A.6    Johnson, E.M.7
  • 33
    • 0027153262 scopus 로고
    • A developmentally regulated DNA-binding protein from mouse brain stimulates myelin basic protein gene expression
    • Haas, S., Gordon, J., and Khalili, K. (1993) A developmentally regulated DNA-binding protein from mouse brain stimulates myelin basic protein gene expression. Mol. Cell. Biol. 13, 3103-3112
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3103-3112
    • Haas, S.1    Gordon, J.2    Khalili, K.3
  • 34
    • 0029100194 scopus 로고
    • A 39-kD DNA-binding protein from mouse brain stimulates transcription of myelin basic protein gene in oligodendrocytic cells
    • Haas, S., Thatikunta, P., Steplewski, A., Johnson, E. M., Khalili, K., and Amini, S. (1995) A 39-kD DNA-binding protein from mouse brain stimulates transcription of myelin basic protein gene in oligodendrocytic cells. J. Cell Biol. 130, 1171-1179
    • (1995) J. Cell Biol. , vol.130 , pp. 1171-1179
    • Haas, S.1    Thatikunta, P.2    Steplewski, A.3    Johnson, E.M.4    Khalili, K.5    Amini, S.6
  • 36
    • 0028972092 scopus 로고
    • Association of human Pur with the retinoblastoma protein, Rb, regulates binding to the single-stranded DNA Pur recognition element
    • Johnson, E. M., Chen, P. L., Krachmarov, C. P., Barr, S. M., Kanovsky, M., Ma, Z. W., and Lee, W. H. (1995) Association of human Pur with the retinoblastoma protein, Rb, regulates binding to the single-stranded DNA Pur recognition element. J. Biol. Chem. 270, 24352-24360
    • (1995) J. Biol. Chem. , vol.270 , pp. 24352-24360
    • Johnson, E.M.1    Chen, P.L.2    Krachmarov, C.P.3    Barr, S.M.4    Kanovsky, M.5    Ma, Z.W.6    Lee, W.H.7
  • 37
    • 0029888999 scopus 로고    scopus 로고
    • Evidence that replication of human neurotropic JC virus DNA in glial cells is regulated by the sequence-specific single-stranded DNA-binding protein Pur
    • Chang, C. F., Gallia, G. L., Muralidharan, V., Chen, N. N., Zoltick, P., Johnson, E., and Khalili, K. (1996) Evidence that replication of human neurotropic JC virus DNA in glial cells is regulated by the sequence-specific single-stranded DNA-binding protein Pur. J. Virol. 70, 4150-4156
    • (1996) J. Virol. , vol.70 , pp. 4150-4156
    • Chang, C.F.1    Gallia, G.L.2    Muralidharan, V.3    Chen, N.N.4    Zoltick, P.5    Johnson, E.6    Khalili, K.7
  • 39
    • 0032575373 scopus 로고    scopus 로고
    • Association of Pur with RNAs homologous to 7 SL determines its binding ability to the myelin basic protein promoter DNA sequence
    • Tretiakova, A., Gallia, G. L., Shcherbik, N., Jameson, B., Johnson, E. M., Amini, S., and Khalili, K. (1998) Association of Pur with RNAs homologous to 7 SL determines its binding ability to the myelin basic protein promoter DNA sequence. J. Biol. Chem. 273, 22241-22247
    • (1998) J. Biol. Chem. , vol.273 , pp. 22241-22247
    • Tretiakova, A.1    Gallia, G.L.2    Shcherbik, N.3    Jameson, B.4    Johnson, E.M.5    Amini, S.6    Khalili, K.7
  • 40
    • 0034257920 scopus 로고    scopus 로고
    • Pur: A multifunctional single-stranded DNA- and RNA-binding protein
    • Gallia, G. L., Johnson, E. M., and Khalili, K. (2000) Pur: a multifunctional single-stranded DNA- and RNA-binding protein. Nucleic Acids Res. 28, 3197-3205
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3197-3205
    • Gallia, G.L.1    Johnson, E.M.2    Khalili, K.3
  • 42
    • 0035803881 scopus 로고    scopus 로고
    • Functional interaction between cyclin T1/cdk9 and Pur determines the level of TNF promoter activation by Tat in glial cells
    • Darbinian, N., Sawaya, B. E., Khalili, K., Jaffe, N., Wortman, B., Giordano, A., and Amini, S. (2001) Functional interaction between cyclin T1/cdk9 and Pur determines the level of TNF promoter activation by Tat in glial cells. J. Neuroimmunol. 121, 3-11
    • (2001) J. Neuroimmunol. , vol.121 , pp. 3-11
    • Darbinian, N.1    Sawaya, B.E.2    Khalili, K.3    Jaffe, N.4    Wortman, B.5    Giordano, A.6    Amini, S.7
  • 43
    • 0034753124 scopus 로고    scopus 로고
    • Single-stranded nucleic acid-binding protein, Pur, interacts with RNA homologous to 18 S ribosomal RNA and inhibits translation in vitro
    • Gallia, G. L., Darbinian, N., Jaffe, N., and Khalili, K. (2001) Single-stranded nucleic acid-binding protein, Pur, interacts with RNA homologous to 18 S ribosomal RNA and inhibits translation in vitro. J. Cell. Biochem. 83, 355-363
    • (2001) J. Cell. Biochem. , vol.83 , pp. 355-363
    • Gallia, G.L.1    Darbinian, N.2    Jaffe, N.3    Khalili, K.4
  • 44
    • 0034746052 scopus 로고    scopus 로고
    • Regulation of Pur gene transcription: Evidence for autoregulation of Pur promoter
    • Muralidharan, V., Sweet, T., Nadraga, Y., Amini, S., and Khalili, K. (2001) Regulation of Pur gene transcription: evidence for autoregulation of Pur promoter. J. Cell Physiol. 186, 406-413
    • (2001) J. Cell Physiol. , vol.186 , pp. 406-413
    • Muralidharan, V.1    Sweet, T.2    Nadraga, Y.3    Amini, S.4    Khalili, K.5
  • 46
    • 34548616504 scopus 로고    scopus 로고
    • Identification of Pur as a new hypoxia response factor responsible for coordinated induction of the 2 integrin family
    • Kong, T., Scully, M., Shelley, C. S., and Colgan, S. P. (2007) Identification of Pur as a new hypoxia response factor responsible for coordinated induction of the 2 integrin family. J. Immunol. 179, 1934-1941
    • (2007) J. Immunol. , vol.179 , pp. 1934-1941
    • Kong, T.1    Scully, M.2    Shelley, C.S.3    Colgan, S.P.4
  • 47
    • 44049092769 scopus 로고    scopus 로고
    • Isolation and characterization of a novel H1.2 complex that acts as a repressor of p53-mediated transcription
    • Kim, K., Choi, J., Heo, K., Kim, H., Levens, D., Kohno, K., Johnson, E. M., Brock, H. W., and An, W. (2008) Isolation and characterization of a novel H1.2 complex that acts as a repressor of p53-mediated transcription. J. Biol. Chem. 283, 9113-9126
    • (2008) J. Biol. Chem. , vol.283 , pp. 9113-9126
    • Kim, K.1    Choi, J.2    Heo, K.3    Kim, H.4    Levens, D.5    Kohno, K.6    Johnson, E.M.7    Brock, H.W.8    An, W.9
  • 49
    • 59449092121 scopus 로고    scopus 로고
    • Multiple roles for Pur in cellular and viral regulation
    • White, M. K., Johnson, E. M., and Khalili, K. (2009) Multiple roles for Pur in cellular and viral regulation. Cell Cycle 8, 1-7
    • (2009) Cell Cycle , vol.8 , pp. 1-7
    • White, M.K.1    Johnson, E.M.2    Khalili, K.3
  • 50
    • 59649126440 scopus 로고    scopus 로고
    • C elegans pur, an activator of end-1, synergizes with the Wnt pathway to specify endoderm
    • Witze, E. S., Field, E. D., Hunt, D. F., and Rothman, J. H. (2009) C. elegans pur, an activator of end-1, synergizes with the Wnt pathway to specify endoderm. Dev. Biol. 327, 12-23
    • (2009) Dev. Biol. , vol.327 , pp. 12-23
    • Witze, E.S.1    Field, E.D.2    Hunt, D.F.3    Rothman, J.H.4
  • 51
    • 77349092321 scopus 로고    scopus 로고
    • Regulation of gonadotropin- releasing hormone-1 gene transcription by members of the purinerich element-binding protein family
    • Zhao, S., Kelm, R. J., Jr., and Fernald, R. D. (2010) Regulation of gonadotropin- releasing hormone-1 gene transcription by members of the purinerich element-binding protein family. Am. J. Physiol. Endocrinol. Metab. 298, E524-E533
    • (2010) Am. J. Physiol. Endocrinol. Metab. , vol.298
    • Zhao, S.1    Kelm Jr., R.J.2    Fernald, R.D.3
  • 52
    • 80053622233 scopus 로고    scopus 로고
    • The purinerich DNA-binding protein OsPur participates in the regulation of the rice sucrose synthase 1 gene expression
    • Chang, J. C., Liao, Y. C., Yang, C. C., and Wang, A. Y. (2011) The purinerich DNA-binding protein OsPur participates in the regulation of the rice sucrose synthase 1 gene expression. Physiol. Plant. 143, 219-234
    • (2011) Physiol. Plant. , vol.143 , pp. 219-234
    • Chang, J.C.1    Liao, Y.C.2    Yang, C.C.3    Wang, A.Y.4
  • 53
    • 84861306825 scopus 로고    scopus 로고
    • Identification of novel DNA-binding proteins using DNA-affinity chromatography/pull down
    • Chapter 1:Unit1F.1. doi:10.1002/9780471729259. mc01f01s24
    • Jutras, B. L., Verma, A., and Stevenson, B. (2012) Identification of novel DNA-binding proteins using DNA-affinity chromatography/pull down. Curr. Protoc. Microbiol. Chapter 1:Unit1F.1. doi:10.1002/9780471729259. mc01f01s24
    • (2012) Curr. Protoc. Microbiol
    • Jutras, B.L.1    Verma, A.2    Stevenson, B.3
  • 54
    • 54749126319 scopus 로고    scopus 로고
    • Laboratory maintenance of Borrelia burgdorferi
    • Chapter 12:Unit12C.1. doi:10.1002/9780471729259. mc12c01s4
    • Zückert,W. R. (2007) Laboratory maintenance of Borrelia burgdorferi. Curr. Protoc. Microbiol. Chapter 12:Unit12C.1. doi:10.1002/9780471729259. mc12c01s4
    • (2007) Curr. Protoc. Microbiol.
    • Zückert, W.R.1
  • 57
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 58
    • 0019878376 scopus 로고
    • Equilibria and kinetics of lac repressor- operator interactions by polyacrylamide gel electrophoresis
    • Fried, M., and Crothers, D. M. (1981) Equilibria and kinetics of lac repressor- operator interactions by polyacrylamide gel electrophoresis. Nucleic Acids Res. 9, 6505-6525
    • (1981) Nucleic Acids Res. , vol.9 , pp. 6505-6525
    • Fried, M.1    Crothers, D.M.2
  • 59
    • 0029906987 scopus 로고    scopus 로고
    • DNA binding mechanism of O6-alkylguanine-DNA alkyltransferase: Stoichiometry and effects of DNA base composition and secondary structure on complex stability
    • Fried, M. G., Kanugula, S., Bromberg, J. L., and Pegg, A. E. (1996) DNA binding mechanism of O6-alkylguanine-DNA alkyltransferase: stoichiometry and effects of DNA base composition and secondary structure on complex stability. Biochemistry 35, 15295-15301
    • (1996) Biochemistry , vol.35 , pp. 15295-15301
    • Fried, M.G.1    Kanugula, S.2    Bromberg, J.L.3    Pegg, A.E.4
  • 62
    • 70349925843 scopus 로고    scopus 로고
    • Development of a single-plasmid-based regulatable gene expression system for Borrelia burgdorferi
    • Whetstine, C. R., Slusser, J. G., and Zückert, W. R. (2009) Development of a single-plasmid-based regulatable gene expression system for Borrelia burgdorferi. Appl. Environ. Microbiol. 75, 6553-6558
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 6553-6558
    • Whetstine, C.R.1    Slusser, J.G.2    Zückert, W.R.3
  • 63
    • 0036042233 scopus 로고    scopus 로고
    • Borrelia burgdorferi-specific monoclonal antibodies derived from mice primed with Lyme disease spirochete-infected Ixodes scapularis ticks
    • Mbow, M. L., Gilmore, R. D., Jr., Stevenson, B., Golde, W. T., Piesman, J., and Johnson, B. J. (2002) Borrelia burgdorferi-specific monoclonal antibodies derived from mice primed with Lyme disease spirochete-infected Ixodes scapularis ticks. Hybrid. Hybridomics 21, 179-182
    • (2002) Hybrid. Hybridomics , vol.21 , pp. 179-182
    • Mbow, M.L.1    Gilmore Jr., R.D.2    Stevenson, B.3    Golde, W.T.4    Piesman, J.5    Johnson, B.J.6
  • 64
  • 65
    • 0028828202 scopus 로고
    • Temperature-related differential expression of antigens in the Lyme disease spirochete, Borrelia burgdorferi
    • Stevenson, B., Schwan, T. G., and Rosa, P. A. (1995) Temperature-related differential expression of antigens in the Lyme disease spirochete, Borrelia burgdorferi. Infect. Immun. 63, 4535-4539
    • (1995) Infect. Immun. , vol.63 , pp. 4535-4539
    • Stevenson, B.1    Schwan, T.G.2    Rosa, P.A.3
  • 66
    • 84873542723 scopus 로고    scopus 로고
    • Changes in bacterial growth rate govern expression of the Borrelia burgdorferi OspC and Erp infection-associated surface proteins
    • Jutras, B. L., Chenail, A. M., and Stevenson, B. (2013) Changes in bacterial growth rate govern expression of the Borrelia burgdorferi OspC and Erp infection-associated surface proteins. J. Bacteriol. 195, 757-764
    • (2013) J. Bacteriol. , vol.195 , pp. 757-764
    • Jutras, B.L.1    Chenail, A.M.2    Stevenson, B.3
  • 67
    • 0031967697 scopus 로고    scopus 로고
    • Oligopeptide permease in Borrelia burgdorferi: Putative peptide-binding components encoded by both chromosomal and plasmid loci
    • Bono, J. L., Tilly, K., Stevenson, B., Hogan, D., and Rosa, P. (1998) Oligopeptide permease in Borrelia burgdorferi: putative peptide-binding components encoded by both chromosomal and plasmid loci. Microbiology 144, 1033-1044
    • (1998) Microbiology , vol.144 , pp. 1033-1044
    • Bono, J.L.1    Tilly, K.2    Stevenson, B.3    Hogan, D.4    Rosa, P.5
  • 68
    • 4644259956 scopus 로고    scopus 로고
    • Genetic exchange and plasmid transfers in Borrelia burgdorferi sensu stricto revealed by three-way genome comparisons and multilocus sequence typing
    • Qiu, W. G., Schutzer, S. E., Bruno, J. F., Attie, O., Xu, Y., Dunn, J. J., Fraser, C. M., Casjens, S. R., and Luft, B. J. (2004) Genetic exchange and plasmid transfers in Borrelia burgdorferi sensu stricto revealed by three-way genome comparisons and multilocus sequence typing. Proc. Natl. Acad. Sci. U.S.A. 101, 14150-14155
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 14150-14155
    • Qiu, W.G.1    Schutzer, S.E.2    Bruno, J.F.3    Attie, O.4    Xu, Y.5    Dunn, J.J.6    Fraser, C.M.7    Casjens, S.R.8    Luft, B.J.9
  • 75
    • 22644452600 scopus 로고    scopus 로고
    • (Smith, M C., and Sockett, R. E., eds) Academic Press, London
    • Rosa, P., Stevenson, B., and Tilly, K. (1999) in Methods in Microbiology (Smith, M. C., and Sockett, R. E., eds) Vol. 29, pp. 209-227, Academic Press, London
    • (1999) Methods in Microbiology , vol.29 , pp. 209-227
    • Rosa, P.1    Stevenson, B.2    Tilly, K.3
  • 76
    • 0029200874 scopus 로고
    • Electrotransformation of the spirochete Borrelia burgdorferi
    • Samuels, D. S. (1995) Electrotransformation of the spirochete Borrelia burgdorferi. Methods Mol. Biol. 47, 253-259
    • (1995) Methods Mol. Biol. , vol.47 , pp. 253-259
    • Samuels, D.S.1
  • 77
    • 0031812086 scopus 로고    scopus 로고
    • Borrelia burgdorferi erp proteins are immunogenic in mammals infected by tick bite, and their synthesis is inducible in cultured bacteria
    • Stevenson, B., Bono, J. L., Schwan, T. G., and Rosa, P. (1998) Borrelia burgdorferi erp proteins are immunogenic in mammals infected by tick bite, and their synthesis is inducible in cultured bacteria. Infect. Immun. 66, 2648-2654
    • (1998) Infect. Immun. , vol.66 , pp. 2648-2654
    • Stevenson, B.1    Bono, J.L.2    Schwan, T.G.3    Rosa, P.4
  • 78
    • 0026253640 scopus 로고
    • Importance of oligoelectrolyte end effects for the thermodynamics of conformational transitions of nucleic acid oligomers: A grand canonical Monte Carlo analysis
    • Olmsted, M. C., Anderson, C. F., and Record, M. T. (1991) Importance of oligoelectrolyte end effects for the thermodynamics of conformational transitions of nucleic acid oligomers: a grand canonical Monte Carlo analysis. Biopolymers 31, 1593-1604
    • (1991) Biopolymers , vol.31 , pp. 1593-1604
    • Olmsted, M.C.1    Anderson, C.F.2    Record, M.T.3
  • 79
    • 15044365667 scopus 로고    scopus 로고
    • Mechanism of DNA binding and localized strand separation by Pur and comparison with Pur family member, Pur beta
    • Wortman, M. J., Johnson, E. M., and Bergemann, A. D. (2005) Mechanism of DNA binding and localized strand separation by Pur and comparison with Pur family member, Pur beta. Biochim. Biophys. Acta 1743, 64-78
    • (2005) Biochim. Biophys. Acta , vol.1743 , pp. 64-78
    • Wortman, M.J.1    Johnson, E.M.2    Bergemann, A.D.3
  • 80
    • 84864590102 scopus 로고    scopus 로고
    • Surface-based and mass spectrometric approaches to deciphering sugar-protein interactions in a galactose-specific agglutinin
    • Jiménez-Castells, C., Defaus, S., Moise, A., Przbylski, M., Andreu, D., and Gutiérrez-Gallego, R. (2012) Surface-based and mass spectrometric approaches to deciphering sugar-protein interactions in a galactose-specific agglutinin. Anal. Chem. 84, 6515-6520
    • (2012) Anal. Chem. , vol.84 , pp. 6515-6520
    • Jiménez-Castells, C.1    Defaus, S.2    Moise, A.3    Przbylski, M.4    Andreu, D.5    Gutiérrez-Gallego, R.6
  • 81
    • 84859563258 scopus 로고    scopus 로고
    • Induced fit on heme binding to the Pseudomonas aeruginosa cytoplasmic protein (PhuS) drives interaction with heme oxygenase (HemO)
    • O'Neill, M. J., Bhakta, M. N., Fleming, K. G., and Wilks, A. (2012) Induced fit on heme binding to the Pseudomonas aeruginosa cytoplasmic protein (PhuS) drives interaction with heme oxygenase (HemO). Proc. Natl. Acad. Sci. 109, 5639-5644
    • (2012) Proc. Natl. Acad. Sci. , vol.109 , pp. 5639-5644
    • O'neill, M.J.1    Bhakta, M.N.2    Fleming, K.G.3    Wilks, A.4
  • 82
    • 84864418203 scopus 로고    scopus 로고
    • Identification and quantification of Fc fusion peptibody degradations by limited proteolysis method
    • Yu, L., Xiao, G., Zhang, J., Remmele, R. L., Jr., Eu, M., and Liu, D. (2012) Identification and quantification of Fc fusion peptibody degradations by limited proteolysis method. Anal. Biochem. 428, 137-142
    • (2012) Anal. Biochem. , vol.428 , pp. 137-142
    • Yu, L.1    Xiao, G.2    Zhang, J.3    Remmele Jr., R.L.4    Eu, M.5    Liu, D.6
  • 84
    • 0024707204 scopus 로고
    • Unusually stable helix formation in short alanine-based peptides
    • Marqusee, S., Robbins, V. H., and Baldwin, R. L. (1989) Unusually stable helix formation in short alanine-based peptides. Proc. Natl. Acad. Sci. U.S.A. 86, 5286-5290
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 5286-5290
    • Marqusee, S.1    Robbins, V.H.2    Baldwin, R.L.3
  • 85
    • 0035393302 scopus 로고    scopus 로고
    • Amino acid-base interactions: A three-dimensional analysis of protein-DNA interactions at an atomic level
    • Luscombe, N. M., Laskowski, R. A., and Thornton, J. M. (2001) Amino acid-base interactions: a three-dimensional analysis of protein-DNA interactions at an atomic level. Nucleic Acids Res. 29, 2860-2874
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2860-2874
    • Luscombe, N.M.1    Laskowski, R.A.2    Thornton, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.