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Volumn 62, Issue 1, 2010, Pages 67-77

Research communication mycobacterial stress regulation: The Dps "twin sister" defense mechanism and structure-function relationship

Author keywords

DNA binding; Dps; Interface cluster analysis; Stress response; Transcriptional regulation

Indexed keywords

DNA BINDING PROTEIN; DPS PROTEIN; BACTERIAL PROTEIN; DPS PROTEIN, BACTERIA;

EID: 77950554012     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (17)

References (63)
  • 1
    • 0036773714 scopus 로고    scopus 로고
    • Synthesis of an unusual polar glycopeptidolipid in glucose-limited culture of Mycobacterium smegmatis
    • Ojha, A. K., Varma, S., and Chatterji, D. (2002) Synthesis of an unusual polar glycopeptidolipid in glucose-limited culture of Mycobacterium smegmatis. Microbiology 148, 3039-3048. (Pubitemid 35243703)
    • (2002) Microbiology , vol.148 , Issue.10 , pp. 3039-3048
    • Ojha, A.K.1    Varma, S.2    Chatterji, D.3
  • 2
  • 3
    • 0033616769 scopus 로고    scopus 로고
    • Evolution of microbial diversity during prolonged starvation
    • Finkel, S. E. and Kolter, R. (1999) Evolution of microbial diversity during prolonged starvation. Proc. Natl. Acad. Sci. USA 96, 4023-4027.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4023-4027
    • Finkel, S.E.1    Kolter, R.2
  • 4
    • 31544474634 scopus 로고    scopus 로고
    • Long-term survival during stationary phase: Evolution and the GASP phenotype
    • Finkel, S. (2006) Long-term survival during stationary phase: evolution and the GASP phenotype. Nat. Rev. Microbiol. 4, 113-120.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 113-120
    • Finkel, S.1
  • 5
    • 25144510071 scopus 로고    scopus 로고
    • Global analysis of proteins synthesized by Mycobacterium smegmatis provides direct evidence for physiological heterogeneity in stationary-phase cultures
    • DOI 10.1128/JB.187.19.6691-6700.2005
    • Blokpoel, M. C. J., Smeulders, M. J., Hubbard, J. A. M., Keer, J., and Williams, H. D. (2005) Global analysis of proteins synthesized by Mycobacterium smegmatis provides direct evidence for physiological heterogeneity in stationary-phase cultures. J. Bacteriol. 187, 6691-6700. (Pubitemid 41356242)
    • (2005) Journal of Bacteriology , vol.187 , Issue.19 , pp. 6691-6700
    • Blokpoel, M.C.J.1    Smeulders, M.J.2    Hubbard, J.A.M.3    Keer, J.4    Williams, H.D.5
  • 6
    • 0036263307 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis genes induced during infection of human macrophages
    • Dubnau, E., Fontán, P., Manganelli, R., Soares-Appel, S., and Smith, I. (2002) Mycobacterium tuberculosis genes induced during infection of human macrophages. Infect. Immun. 70, 2787-2795.
    • (2002) Infect. Immun. , vol.70 , pp. 2787-2795
    • Dubnau, E.1    Fontán, P.2    Manganelli, R.3    Soares-Appel, S.4    Smith, I.5
  • 8
    • 7944221099 scopus 로고    scopus 로고
    • What do microarrays really tell us about M. tuberculosis?
    • DOI 10.1016/j.tim.2004.10.005, PII S0966842X04002367
    • Kendall, S. L., Rison, S. C., Movahedzadeh, F., Frita, R., and Stoker, N. G. (2004) What do microarrays really tell us about M. tuberculosis? Trends. Microbiol 12, 537-544. (Pubitemid 39469902)
    • (2004) Trends in Microbiology , vol.12 , Issue.12 , pp. 537-544
    • Kendall, S.L.1    Rison, S.C.G.2    Movahedzadeh, F.3    Frita, R.4    Stoker, N.G.5
  • 9
    • 33750454114 scopus 로고    scopus 로고
    • Comparative transcriptional analysis of human macrophages exposed to animal and human isolates of Mycobacterium avium subspecies paratuberculosis with diverse genotypes
    • Motiwala, A. S., Janagama, H. K., Paustian, M. L., Zhu, X., Bannantine, J. P., Kapur, V., and Sreevatsan, S. (2006) Comparative transcriptional analysis of human macrophages exposed to animal and human isolates of Mycobacterium avium subspecies paratuberculosis with diverse genotypes. Infect. Immun. 74, 6046-6056.
    • (2006) Infect. Immun. , vol.74 , pp. 6046-6056
    • Motiwala, A.S.1    Janagama, H.K.2    Paustian, M.L.3    Zhu, X.4    Bannantine, J.P.5    Kapur, V.6    Sreevatsan, S.7
  • 10
    • 33748621460 scopus 로고    scopus 로고
    • Transcriptional profile of the immune response in the lungs of patients with active tuberculosis
    • Grassi, M., Bocchino, M., Marruchella, A., Volpe, E., Saltini, C., Colizzi, V., and Mariani, F. (2006) Transcriptional profile of the immune response in the lungs of patients with active tuberculosis. Clin. Immunol. 121, 100-107.
    • (2006) Clin. Immunol. , vol.121 , pp. 100-107
    • Grassi, M.1    Bocchino, M.2    Marruchella, A.3    Volpe, E.4    Saltini, C.5    Colizzi, V.6    Mariani, F.7
  • 11
    • 34249795472 scopus 로고    scopus 로고
    • Transcriptomic analysis identifies growth rate modulation as a component of the adaptation of mycobacteria to survival inside the macrophage
    • DOI 10.1128/JB.01787-06
    • Beste, D. J., Laing, E., Bonde, B., Avignone-Rossa, C., Bushell, M. E., and Mcfadden, J. J. (2007) Transcriptomic analysis identifies growth rate modulation as a component of the adaptation of mycobacteria to survival inside the macrophage. J. Bacteriol. 189, 3969-3976. (Pubitemid 46847343)
    • (2007) Journal of Bacteriology , vol.189 , Issue.11 , pp. 3969-3976
    • Beste, D.J.V.1    Laing, E.2    Bonde, B.3    Avignone-Rossa, C.4    Bushell, M.E.5    McFadden, J.J.6
  • 14
    • 54849439916 scopus 로고    scopus 로고
    • Transcriptional analysis of diverse strains Mycobacterium avium subspecies paratuberculosis in primary bovine monocyte derived macrophages
    • Zhu, X., Tu, Z. J., Coussens, P. M., Kapur, V., Janagama, H., Naser, S., and Sreevatsan, S. (2008) Transcriptional analysis of diverse strains Mycobacterium avium subspecies paratuberculosis in primary bovine monocyte derived macrophages. Microbes Infect 10, 1274-1282.
    • (2008) Microbes Infect , vol.10 , pp. 1274-1282
    • Zhu, X.1    Tu, Z.J.2    Coussens, P.M.3    Kapur, V.4    Janagama, H.5    Naser, S.6    Sreevatsan, S.7
  • 15
    • 1842585499 scopus 로고    scopus 로고
    • The temporal expression profile of Mycobacterium tuberculosis infection in mice
    • Talaat, A. M., Lyons, R., Howard, S. T., and Johnston, S. A. (2004) The temporal expression profile of Mycobacterium tuberculosis infection in mice. Proc. Natl. Acad. Sci. USA 101, 4602-4607.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4602-4607
    • Talaat, A.M.1    Lyons, R.2    Howard, S.T.3    Johnston, S.A.4
  • 18
    • 0030811135 scopus 로고    scopus 로고
    • Protection of DNA during oxidative stress by the nonspecific DNA- Binding protein Dps
    • Martinez, A. and Kolter, R. (1997) Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps. J. Bacteriol. 179, 5188-5194. (Pubitemid 27340555)
    • (1997) Journal of Bacteriology , vol.179 , Issue.16 , pp. 5188-5194
    • Martinez, A.1    Kolter, R.2
  • 19
    • 70350176497 scopus 로고    scopus 로고
    • Streptomyces coelicolor Dps-like proteins: Differential dual roles in response to stress during vegetative growth and in nucleoid condensation during reproductive cell division
    • Facey, P. D., Hitchings, M. D., Saavedra-Garcia, P., Fernandez- Martinez, L., Dyson, P. J., and Del Sol, R. (2009) Streptomyces coelicolor Dps-like proteins: differential dual roles in response to stress during vegetative growth and in nucleoid condensation during reproductive cell division. Mol. Microbiol. 73, 1186-1202.
    • (2009) Mol. Microbiol. , vol.73 , pp. 1186-1202
    • Facey, P.D.1    Hitchings, M.D.2    Saavedra-Garcia, P.3    Fernandez- Martinez, L.4    Dyson, P.J.5    Del Sol, R.6
  • 20
    • 65149086817 scopus 로고    scopus 로고
    • Crystal structure of E. coli RecE protein reveals a toroidal tetramer for processing double- stranded DNA breaks
    • Zhang, J., Xing, X., Herr, A. B., and Bell, C. E. (2009) Crystal structure of E. coli RecE protein reveals a toroidal tetramer for processing double- stranded DNA breaks. Structure 17, 690-702.
    • (2009) Structure , vol.17 , pp. 690-702
    • Zhang, J.1    Xing, X.2    Herr, A.B.3    Bell, C.E.4
  • 21
    • 67650273080 scopus 로고    scopus 로고
    • Stepwise evolution of the herpes simplex virus origin binding protein and origin of replication
    • Olsson, M., Tang, K. W., Persson, C., Wilhelmsson, L. M., Billeter, M., and Elias, P. (2009) Stepwise evolution of the herpes simplex virus origin binding protein and origin of replication. J. Biol. Chem. 284, 16246-16255.
    • (2009) J. Biol. Chem. , vol.284 , pp. 16246-16255
    • Olsson, M.1    Tang, K.W.2    Persson, C.3    Wilhelmsson, L.M.4    Billeter, M.5    Elias, P.6
  • 22
    • 62549160340 scopus 로고    scopus 로고
    • Rad52 promotes second-end DNA capture in double-stranded break repair to form complement-stabilized joint molecules
    • Nimonkar, A. V., Sica, R. A., and Kowalczykowski, S. C. (2009) Rad52 promotes second-end DNA capture in double-stranded break repair to form complement-stabilized joint molecules. Proc. Natl. Acad. Sci. USA 106, 3077-3082.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 3077-3082
    • Nimonkar, A.V.1    Sica, R.A.2    Kowalczykowski, S.C.3
  • 23
    • 0027083350 scopus 로고
    • A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli
    • Almirón, M., Link, A. J., Furlong, D., and Kolter, R. (1992) A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. Genes Dev 6, 2646-2654. (Pubitemid 23052891)
    • (1992) Genes and Development , vol.6 , Issue.12 B , pp. 2646-2654
    • Almiron, M.1    Link, A.J.2    Furlong, D.3    Kolter, R.4
  • 24
    • 0038813712 scopus 로고    scopus 로고
    • Bimodal protection of DNA by Mycobacterium smegmatis DNA-binding protein from stationary phase cells
    • Gupta, S. and Chatterji, D. (2003) Bimodal protection of DNA by Mycobacterium smegmatis DNA-binding protein from stationary phase cells. J. Biol. Chem. 278, 5235-5241.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5235-5241
    • Gupta, S.1    Chatterji, D.2
  • 25
    • 0842269876 scopus 로고    scopus 로고
    • Identification of an iron-binding protein of the Dps family expressed by Streptococcus thermophilus
    • Nicodème, M., Perrin, C., Hols, P., Bracquart, P., and Gaillard, J. L. (2004) Identification of an iron-binding protein of the Dps family expressed by Streptococcus thermophilus. Curr. Microbiol. 48, 51-56.
    • (2004) Curr. Microbiol. , vol.48 , pp. 51-56
    • Nicodème, M.1    Perrin, C.2    Hols, P.3    Bracquart, P.4    Gaillard, J.L.5
  • 27
    • 33644859833 scopus 로고    scopus 로고
    • Emergence of biofilm-forming subpopulations upon exposure of Escherichia coli to environmental bacteriophages
    • Lacqua, A., Wanner, O., Colangelo, T., Martinotti, M. G., and Landini, P. (2006) Emergence of biofilm-forming subpopulations upon exposure of Escherichia coli to environmental bacteriophages. Appl. Environ. Microbiol. 72, 956-959.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 956-959
    • Lacqua, A.1    Wanner, O.2    Colangelo, T.3    Martinotti, M.G.4    Landini, P.5
  • 30
    • 0034780485 scopus 로고    scopus 로고
    • Nonreplicating persistence of Mycobacterium tuberculosis
    • Wayne, L. and Sohaskey, C. (2001) Nonreplicating persistence of Mycobacterium tuberculosis. Annu. Rev. Microbiol. 55, 139-163.
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 139-163
    • Wayne, L.1    Sohaskey, C.2
  • 31
    • 0016159839 scopus 로고
    • Studies on the effect of starvation on mycobacteria
    • Nyka, W. (1974) Studies on the effect of starvation on mycobacteria. Infect. Immun. 9, 843-850.
    • (1974) Infect. Immun. , vol.9 , pp. 843-850
    • Nyka, W.1
  • 33
    • 33745909152 scopus 로고    scopus 로고
    • Crystal structure of Dps-1, a functionally distinct Dps protein from Deinococcus radiodurans
    • Kim, S. G., Bhattacharyya, G., Grove, A., and Lee, Y. H. (2006) Crystal structure of Dps-1, a functionally distinct Dps protein from Deinococcus radiodurans. J. Mol. Biol. 361, 105-114.
    • (2006) J. Mol. Biol. , vol.361 , pp. 105-114
    • Kim, S.G.1    Bhattacharyya, G.2    Grove, A.3    Lee, Y.H.4
  • 34
    • 34447622836 scopus 로고    scopus 로고
    • The crystal structure of the Dps2 from Deinococcus radiodurans reveals an unusual pore profile with a non-specific metal binding site
    • Cuypers, M. G., Mitchell, E. P., Romão, C. V., and Mcsweeney, S. M. (2007) The crystal structure of the Dps2 from Deinococcus radiodurans reveals an unusual pore profile with a non-specific metal binding site. J. Mol. Biol. 371, 787-799.
    • (2007) J. Mol. Biol. , vol.371 , pp. 787-799
    • Cuypers, M.G.1    Mitchell, E.P.2    Romão, C.V.3    Mcsweeney, S.M.4
  • 35
    • 0030665283 scopus 로고    scopus 로고
    • Expression of a stress- and starvation-induced dps/pexB-homologous gene is controlled by the alternative sigma factor sigma(B) in Bacillus subtilis
    • Antelmann, H., Engelmann, S., Schmid, R., Sorokin, A., Lapidus, A., and Hecker, M. (1997) Expression of a stress- and starvation-induced dps/pexB-homologous gene is controlled by the alternative Sigma Factor sigmaB in Bacillus subtilis. J. Bacteriol. 179, 7251-7256. (Pubitemid 27509960)
    • (1997) Journal of Bacteriology , vol.179 , Issue.23 , pp. 7251-7256
    • Antelmann, H.1    Engelmann, S.2    Schmid, R.3    Sorokin, A.4    Lapidus, A.5    Hecker, M.6
  • 37
    • 3042582299 scopus 로고    scopus 로고
    • X-ray analysis of Mycobacterium smegmatis Dps and a comparative study involving other Dps and Dps-like molecules
    • Roy, S., Gupta, S., Das, S., Sekar, K., Chatterji, D., and Vijayan, M. (2004) X-ray analysis of Mycobacterium smegmatis Dps and a comparative study involving other Dps and Dps-like molecules. J. Mol. Biol. 339, 1103-1113.
    • (2004) J. Mol. Biol. , vol.339 , pp. 1103-1113
    • Roy, S.1    Gupta, S.2    Das, S.3    Sekar, K.4    Chatterji, D.5    Vijayan, M.6
  • 38
    • 37349040333 scopus 로고    scopus 로고
    • Structural studies on the second Mycobacterium smegmatis Dps: Invariant and variable features of structure, assembly and function
    • Roy, S., Saraswathi, R., Chatterji, D., and Vijayan, M. (2008) Structural studies on the second Mycobacterium smegmatis Dps: invariant and variable features of structure, assembly and function. J. Mol. Biol. 375, 948-959.
    • (2008) J. Mol. Biol. , vol.375 , pp. 948-959
    • Roy, S.1    Saraswathi, R.2    Chatterji, D.3    Vijayan, M.4
  • 39
    • 33748878031 scopus 로고    scopus 로고
    • Paired Bacillus anthracis Dps (mini-ferritin) have different reactivities with peroxide
    • Liu, X., Kim, K., Leighton, T., and Theil, E. C. (2006) Paired Bacillus anthracis Dps (mini-ferritin) have different reactivities with peroxide. J. Biol. Chem. 281, 27827-27835.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27827-27835
    • Liu, X.1    Kim, K.2    Leighton, T.3    Theil, E.C.4
  • 40
    • 34249941286 scopus 로고    scopus 로고
    • Role of N and C-terminal tails in DNA binding and assembly in Dps: Structural studies of Mycobacterium smegmatis Dps deletion mutants
    • Roy, S., Saraswathi, R., Gupta, S., Sekar, K., Chatterji, D., and Vijayan, M. (2007) Role of N and C-terminal tails in DNA binding and assembly in Dps: structural studies of Mycobacterium smegmatis Dps deletion mutants. J. Mol. Biol. 370, 752-767,
    • (2007) J. Mol. Biol. , vol.370 , pp. 752-767
    • Roy, S.1    Saraswathi, R.2    Gupta, S.3    Sekar, K.4    Chatterji, D.5    Vijayan, M.6
  • 41
    • 0028181132 scopus 로고
    • Characterization of the sigma38-dependent expression of a core Escherichia coli starvation gene, pexB
    • Lomovskaya, O. L., Kidwell, J. P., and Matin, A. (1994) Characterization of the sigma 38-dependent expression of a core Escherichia coli starvation gene, pexB. J. Bacteriol. 176, 3928-3935, (Pubitemid 2106801)
    • (1994) Journal of Bacteriology , vol.176 , Issue.13 , pp. 3928-3935
    • Lomovskaya, O.L.1    Kidwell, J.P.2    Matin, A.3
  • 42
    • 44249126516 scopus 로고    scopus 로고
    • Selective repression by Fis and H-NS at the Escherichia colidps promoter
    • Grainger, D. C., Goldberg, M. D., Lee, D. J., and Busby, S. J. W. (2008) Selective repression by Fis and H-NS at the Escherichia colidps promoter. Mol. Microbiol. 68, 1366-1377,
    • (2008) Mol. Microbiol. , vol.68 , pp. 1366-1377
    • Grainger, D.C.1    Goldberg, M.D.2    Lee, D.J.3    Busby, S.J.W.4
  • 43
    • 44249112381 scopus 로고    scopus 로고
    • Fine-tuned growth phase control of dps, encoding a DNA protection protein, by FIS and H-NS
    • Schnetz, K. (2008) Fine-tuned growth phase control of dps, encoding a DNA protection protein, by FIS and H-NS. Mol. Microbiol. 68, 1345-1347,
    • (2008) Mol. Microbiol. , vol.68 , pp. 1345-1347
    • Schnetz, K.1
  • 44
    • 0141566368 scopus 로고    scopus 로고
    • Dynamic control of Dps protein levels by ClpXP and ClpAP proteases in Escherichia coli
    • Stephani, K., Weichart, D., and Hengge, R. (2003) Dynamic control of Dps protein levels by ClpXP and ClpAP proteases in Escherichia coli. Mol. Microbiol. 49, 1605-1614,
    • (2003) Mol. Microbiol. , vol.49 , pp. 1605-1614
    • Stephani, K.1    Weichart, D.2    Hengge, R.3
  • 45
    • 0036019356 scopus 로고    scopus 로고
    • Proteomics analysis of carbon-starved Mycobacterium smegmatis: Induction of Dps-like protein
    • Gupta, S., Pandit, S. B., Srinivasan, N., and Chatterji, D. (2002) Proteomics analysis of carbon-starved Mycobacterium smegmatis: induction of Dps-like protein. Protein. Eng. 15, 503-512,
    • (2002) Protein. Eng. , vol.15 , pp. 503-512
    • Gupta, S.1    Pandit, S.B.2    Srinivasan, N.3    Chatterji, D.4
  • 46
    • 0005443595 scopus 로고
    • Reconstitution of bacterial DNA-dependent RNA-polymerase from isolated subunits as a tool for the elucidation of the role of the subunits in transcription
    • Heil, A. and Zillig, W. (1970) Reconstitution of bacterial DNA-dependent RNA-polymerase from isolated subunits as a tool for the elucidation of the role of the subunits in transcription. FEBS Lett. 11, 165-168.
    • (1970) FEBS Lett. , vol.11 , pp. 165-168
    • Heil, A.1    Zillig, W.2
  • 47
    • 0015506575 scopus 로고
    • Subunits of RNA polymerase in function and structure. II. Reconstitution of Escherichia coli RNA polymerase from isolated subunits
    • Ishihama, A. and Ito, K. (1972) Subunits of RNA polymerase in function and structure. II. Reconstitution of Escherichia coli RNA polymerase from isolated subunits. J. Mol. Biol. 72, 111-123.
    • (1972) J. Mol. Biol. , vol.72 , pp. 111-123
    • Ishihama, A.1    Ito, K.2
  • 48
    • 0029797365 scopus 로고    scopus 로고
    • Reconstitution of RNA polymerase
    • Fujita, N. and Ishihama, A. (1996) Reconstitution of RNA polymerase. Meth. Enzymol. 273, 121-130,
    • (1996) Meth. Enzymol. , vol.273 , pp. 121-130
    • Fujita, N.1    Ishihama, A.2
  • 49
    • 33645532080 scopus 로고    scopus 로고
    • Posttranslational regulation of Mycobacterium tuberculosis extracytoplasmic-function sigma factor sigma L and roles in virulence and in global regulation of gene expression
    • Dainese, E., Rodrigue, S., Delogu, G., Provvedi, R., Laflamme, L., Brzezinski, R., Fadda, G., Smith, I., Gaudreau, L., Palù, G., and Manganelli, R. (2006) Posttranslational regulation of Mycobacterium tuberculosis extracytoplasmic-function sigma factor sigma L and roles in virulence and in global regulation of gene expression. Infect. Immun. 74, 2457-2461,
    • (2006) Infect. Immun. , vol.74 , pp. 2457-2461
    • Dainese, E.1    Rodrigue, S.2    Delogu, G.3    Provvedi, R.4    Laflamme, L.5    Brzezinski, R.6    Fadda, G.7    Smith, I.8    Gaudreau, L.9    Palù, G.10    Manganelli, R.11
  • 50
    • 38849201790 scopus 로고    scopus 로고
    • Cascade of extracytoplasmic function sigma factors in Mycobacterium tuberculosis: Identification of a sigmaJ-dependent promoter upstream of sigI FEMS
    • Homerova, D., Halgasova, L., and Kormanec, J. (2008) Cascade of extracytoplasmic function sigma factors in Mycobacterium tuberculosis: identification of a sigmaJ-dependent promoter upstream of sigI FEMS. Microbiol. Lett. 280, 120-126,
    • (2008) Microbiol. Lett. , vol.280 , pp. 120-126
    • Homerova, D.1    Halgasova, L.2    Kormanec, J.3
  • 51
    • 0038291700 scopus 로고    scopus 로고
    • The multi-layered structure of Dps with a novel di-nuclear ferroxidase center
    • Ren, B., Tibbelin, G., Kajino, T., Asami, O., and Ladenstein, R. (2003) The multi-layered structure of Dps with a novel di-nuclear ferroxidase center. J. Mol. Biol. 329, 467-477.
    • (2003) J. Mol. Biol. , vol.329 , pp. 467-477
    • Ren, B.1    Tibbelin, G.2    Kajino, T.3    Asami, O.4    Ladenstein, R.5
  • 52
    • 0033986734 scopus 로고    scopus 로고
    • The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site
    • Ilari, A., Stefanini, S., Chiancone, E., and Tsernoglou, D. (2000) The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site. Nat. Struct. Biol. 7, 38-43.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 38-43
    • Ilari, A.1    Stefanini, S.2    Chiancone, E.3    Tsernoglou, D.4
  • 53
    • 0037008743 scopus 로고    scopus 로고
    • Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritinlike DNA-binding protein of Escherichia coli
    • Zhao, G., Ceci, P., Ilari, A., Giangiacomo, L., Laue, T. M., Chiancone, E., and Chasteen, N. D. (2002) Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritinlike DNA-binding protein of Escherichia coli. J. Biol. Chem. 277, 27689-27696.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27689-27696
    • Zhao, G.1    Ceci, P.2    Ilari, A.3    Giangiacomo, L.4    Laue, T.M.5    Chiancone, E.6    Chasteen, N.D.7
  • 54
    • 10244243805 scopus 로고    scopus 로고
    • DNA condensation and self-aggregation of Escherichia coli Dps are coupled phenomena related to the properties of the N-terminus
    • Ceci, P., Cellai, S., Falvo, E., Rivetti, C., Rossi, G. L., and Chiancone, E. (2004) DNA condensation and self-aggregation of Escherichia coli Dps are coupled phenomena related to the properties of the N-terminus. Nucl. Acids. Res. 32, 5935-5944.
    • (2004) Nucl. Acids. Res. , vol.32 , pp. 5935-5944
    • Ceci, P.1    Cellai, S.2    Falvo, E.3    Rivetti, C.4    Rossi, G.L.5    Chiancone, E.6
  • 55
    • 34249725630 scopus 로고    scopus 로고
    • The N-terminal extensions of Deinococcus radiodurans Dps-1 mediate DNA major groove interactions as well as assembly of the dodecamer
    • Bhattacharyya, G. and Grove, A. (2007) The N-terminal extensions of Deinococcus radiodurans Dps-1 mediate DNA major groove interactions as well as assembly of the dodecamer. J. Biol. Chem. 282, 11921-11930.
    • (2007) J. Biol. Chem. , vol.282 , pp. 11921-11930
    • Bhattacharyya, G.1    Grove, A.2
  • 56
    • 33748372577 scopus 로고    scopus 로고
    • The crystal structure of Deinococcus radiodurans Dps protein (DR2263) reveals the presence of a novel metal centre in the N terminus
    • Romão, C., Mitchell, E., and Mcsweeney, S. (2006) The crystal structure of Deinococcus radiodurans Dps protein (DR2263) reveals the presence of a novel metal centre in the N terminus. J. Biol. Inorg. Chem. 11, 891-902.
    • (2006) J. Biol. Inorg. Chem. , vol.11 , pp. 891-902
    • Romão, C.1    Mitchell, E.2    Mcsweeney, S.3
  • 57
    • 34247590894 scopus 로고    scopus 로고
    • Estimation of Förster's distance between two ends of Dps protein from mycobacteria: Distance heterogeneity as a function of oligomerization and DNA binding
    • Chowdhury, R. P. and Chatterji, D. (2007) Estimation of Förster's distance between two ends of Dps protein from mycobacteria: distance heterogeneity as a function of oligomerization and DNA binding. Biophys. Chem. 128, 19-29.
    • (2007) Biophys. Chem. , vol.128 , pp. 19-29
    • Chowdhury, R.P.1    Chatterji, D.2
  • 59
    • 33847067891 scopus 로고    scopus 로고
    • Asn disrupt an intersubunit salt bridge and convert Listeria innocua Dps into its natural mutant Listeria monocytogenes Dps Effects on Protein Stability at Low pH
    • Bellapadrona, G., Chiaraluce, R., Consalvi, V., Ilari, A., Stefanini, S., and Chiancone, E. (2007) Asn disrupt an intersubunit salt bridge and convert Listeria innocua Dps into its natural mutant Listeria monocytogenes Dps Effects on Protein Stability at Low pH. Proteins 66, 975-983.
    • (2007) Proteins , vol.66 , pp. 975-983
    • Bellapadrona, G.1    Chiaraluce, R.2    Consalvi, V.3    Ilari, A.4    Stefanini, S.5    Chiancone, E.6
  • 60
    • 34447503697 scopus 로고    scopus 로고
    • Conformational entropy in molecular recognition by proteins
    • Frederick, K. K., Marlow, M. S., Valentine, K. G., and Wand, A. J. (2007) Conformational entropy in molecular recognition by proteins. Nature 448, 325-329.
    • (2007) Nature , vol.448 , pp. 325-329
    • Frederick, K.K.1    Marlow, M.S.2    Valentine, K.G.3    Wand, A.J.4
  • 61
    • 0036893020 scopus 로고    scopus 로고
    • Side-chain conformational entropy at protein-protein interfaces
    • DOI 10.1110/ps.0222702
    • Cole, C. and Warwicker, J. (2002) Side-chain conformational entropy at protein-protein interfaces. Protein Sci. 11, 2860-2870. (Pubitemid 35365252)
    • (2002) Protein Science , vol.11 , Issue.12 , pp. 2860-2870
    • Cole, C.1    Warwicker, J.2
  • 62
    • 54449101143 scopus 로고    scopus 로고
    • Molecular mechanism of in vitro oligomerization of Dps from Mycobacterium smegmatis: Mutations of the residues identified by "interface cluster" analysis
    • Chowdhury, R., Vijayabaskar, M., Vishveshwara, S., and Chatterji, D. (2008) Molecular mechanism of in vitro oligomerization of Dps from Mycobacterium smegmatis: mutations of the residues identified by "interface cluster" analysis. Biochemistry 47, 11110-11117.
    • (2008) Biochemistry , vol.47 , pp. 11110-11117
    • Chowdhury, R.1    Vijayabaskar, M.2    Vishveshwara, S.3    Chatterji, D.4
  • 63
    • 77949422340 scopus 로고    scopus 로고
    • Protein cages, rings and tubes: Useful components of future nanodevices?
    • Heddle, J. G. (2008) Protein cages, rings and tubes: useful components of future nanodevices? Nanotechnol. Sci. Appl. 1, 67-78.
    • (2008) Nanotechnol. Sci. Appl. , vol.1 , pp. 67-78
    • Heddle, J.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.