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Volumn 34, Issue 22, 2006, Pages 6708-6717

3D structure of Thermus aquaticus single-stranded DNA-binding protein gives insight into the functioning of SSB proteins

Author keywords

[No Author keywords available]

Indexed keywords

DNA DIRECTED DNA POLYMERASE ALPHA; MUTANT PROTEIN; PROLINE; SINGLE STRANDED DNA BINDING PROTEIN;

EID: 33845874427     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkl1002     Document Type: Article
Times cited : (32)

References (47)
  • 1
    • 13444282478 scopus 로고    scopus 로고
    • PriA helicase and SSB interact physically and functionally
    • Cadman,C.J. and McGlynn,P. (2004) PriA helicase and SSB interact physically and functionally. Nucleic Acids Res., 32, 6378-6387.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 6378-6387
    • Cadman, C.J.1    McGlynn, P.2
  • 2
    • 0034074478 scopus 로고    scopus 로고
    • Interaction of E.coli single-stranded DNA binding protein (SSB) with exonuclease I. The carboxy-terminus of SSB is the recognition site for the nuclease
    • Genschel,J., Curth,U. and Urbanke,C. (2000) Interaction of E.coli single-stranded DNA binding protein (SSB) with exonuclease I. The carboxy-terminus of SSB is the recognition site for the nuclease. Biol. Chem., 381, 183-192.
    • (2000) Biol. Chem. , vol.381 , pp. 183-192
    • Genschel, J.1    Curth, U.2    Urbanke, C.3
  • 3
    • 0035907374 scopus 로고    scopus 로고
    • Chimeras between single-stranded DNA-binding proteins from Escherichia coli and Mycobacterium tuberculosis reveal that their C-terminal domains interact with Uracil DNA Glycosylases
    • Handa,P., Acharya,N. and Varshney,U. (2001) Chimeras between single-stranded DNA-binding proteins from Escherichia coli and Mycobacterium tuberculosis reveal that their C-terminal domains interact with Uracil DNA Glycosylases. J. Biol. Chem., 276, 16992-16997.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16992-16997
    • Handa, P.1    Acharya, N.2    Varshney, U.3
  • 4
    • 0032522760 scopus 로고    scopus 로고
    • Devoted to the lagging strand - The subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly
    • Kelman,Z., Yuzhakov,A., Andjelkovic,J. and O'Donnell,M. (1998) Devoted to the lagging strand - the subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly. EMBO J., 17, 2436-2449.
    • (1998) EMBO J. , vol.17 , pp. 2436-2449
    • Kelman, Z.1    Yuzhakov, A.2    Andjelkovic, J.3    O'Donnell, M.4
  • 5
    • 0043163774 scopus 로고    scopus 로고
    • DNA polymerase III chi subunit ties single-stranded DNA binding protein to the bacterial replication machinery
    • Witte,G., Urbanke,C. and Curth,U. (2003) DNA polymerase III chi subunit ties single-stranded DNA binding protein to the bacterial replication machinery. Nucleic Acids Res., 31, 4434-4440.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4434-4440
    • Witte, G.1    Urbanke, C.2    Curth, U.3
  • 6
    • 0033534380 scopus 로고    scopus 로고
    • Trading places on DNA - A three-point switch underlies primer handoff from primase to the replicative DNA polymerase
    • Yuzhakov,A., Kelman,Z. and O'Donnell,M. (1999) Trading places on DNA - a three-point switch underlies primer handoff from primase to the replicative DNA polymerase. Cell, 96, 153-163.
    • (1999) Cell , vol.96 , pp. 153-163
    • Yuzhakov, A.1    Kelman, Z.2    O'Donnell, M.3
  • 7
    • 0025055526 scopus 로고
    • Use of the Escherichia coli ssb gene to prevent bioreactor takeover by plasmidless cells
    • Porter,R., Black,S., Pannuri,S. and Carlson,A. (1990) Use of the Escherichia coli ssb gene to prevent bioreactor takeover by plasmidless cells. BioTechnology, 8, 47-51.
    • (1990) BioTechnology , vol.8 , pp. 47-51
    • Porter, R.1    Black, S.2    Pannuri, S.3    Carlson, A.4
  • 8
    • 0029789824 scopus 로고    scopus 로고
    • A minimal gene set for cellular life derived by comparison of complete bacterial genomes
    • Mushegian,A.R. and Koonin,E.V. (1996) A minimal gene set for cellular life derived by comparison of complete bacterial genomes. Proc. Natl Acad. Sci. USA, 93, 10268-10273.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 10268-10273
    • Mushegian, A.R.1    Koonin, E.V.2
  • 9
    • 0027479161 scopus 로고
    • OB(oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • Murzin,A.G. (1993) OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. EMBO J., 12, 861-867.
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 10
    • 0036753999 scopus 로고    scopus 로고
    • A dimeric mutant of the homotetrameric single-stranded DNA binding protein from Escherichia coli
    • Landwehr,M., Curth,U. and Urbanke,C. (2002) A dimeric mutant of the homotetrameric single-stranded DNA binding protein from Escherichia coli. Biol. Chem., 383, 1325-1333.
    • (2002) Biol. Chem. , vol.383 , pp. 1325-1333
    • Landwehr, M.1    Curth, U.2    Urbanke, C.3
  • 11
    • 0036772213 scopus 로고    scopus 로고
    • Identification and characterization of single-stranded-DNA-binding proteins from Thermus thermophilus and Thermus aquaticus - New arrangement of binding domains
    • Dabrowski,S., Olszewski,M., Piatek,R., Brillowska-Dabrowska,A., Konopa,G. and Kur,J. (2002) Identification and characterization of single-stranded-DNA-binding proteins from Thermus thermophilus and Thermus aquaticus - new arrangement of binding domains. Microbiology, 148, 3307-3315.
    • (2002) Microbiology , vol.148 , pp. 3307-3315
    • Dabrowski, S.1    Olszewski, M.2    Piatek, R.3    Brillowska-Dabrowska, A.4    Konopa, G.5    Kur, J.6
  • 12
    • 2942642109 scopus 로고    scopus 로고
    • The single-stranded DNA-binding protein of Deinococcus radiodurans
    • Eggington,J.M., Haruta,N., Wood,E.A. and Cox,M.M. (2004) The single-stranded DNA-binding protein of Deinococcus radiodurans. BMC Microbiol., 4, 2.
    • (2004) BMC Microbiol. , vol.4 , pp. 2
    • Eggington, J.M.1    Haruta, N.2    Wood, E.A.3    Cox, M.M.4
  • 13
    • 15044347420 scopus 로고    scopus 로고
    • Single-stranded DNA-binding protein of Deinococcus radiodurans: A biophysical characterization
    • Witte,G., Urbanke,C. and Curth,U. (2005) Single-stranded DNA-binding protein of Deinococcus radiodurans: A biophysical characterization. Nucleic Acids Res., 33, 1662-1670.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 1662-1670
    • Witte, G.1    Urbanke, C.2    Curth, U.3
  • 14
    • 2942597631 scopus 로고    scopus 로고
    • Crystal structure of the Deinococcus radiodurans single-stranded DNA-binding protein suggests a mechanism for coping with DNA damage
    • Bernstein,D.A., Eggington,J.M., Killoran,M.P., Misic,A.M., Cox,M.M. and Keck,J.L. (2004) Crystal structure of the Deinococcus radiodurans single-stranded DNA-binding protein suggests a mechanism for coping with DNA damage. Proc. Natl Acad. Sci. USA, 101, 8575-8580.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 8575-8580
    • Bernstein, D.A.1    Eggington, J.M.2    Killoran, M.P.3    Misic, A.M.4    Cox, M.M.5    Keck, J.L.6
  • 15
    • 0034092927 scopus 로고    scopus 로고
    • Roles of functional loops and the C-terminal segment of a single-stranded DNA binding protein elucidated by X-Ray structure analysis
    • Matsumoto,T., Morimoto,Y., Shibata,N., Kinebuchi,T., Shimamoto,N., Tsukihara,T. and Yasuoka,N. (2000) Roles of functional loops and the C-terminal segment of a single-stranded DNA binding protein elucidated by X-Ray structure analysis. J. Biochem. (Tokyo), 127, 329-335.
    • (2000) J. Biochem. (Tokyo) , vol.127 , pp. 329-335
    • Matsumoto, T.1    Morimoto, Y.2    Shibata, N.3    Kinebuchi, T.4    Shimamoto, N.5    Tsukihara, T.6    Yasuoka, N.7
  • 16
    • 0031009811 scopus 로고    scopus 로고
    • Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2.9Å resolution
    • Raghunathan,S., Ricard,C.S., Lohman,T.M. and Waksman,G. (1997) Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2.9Å resolution. Proc. Natl Acad. Sci. USA, 94, 6652-6657.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 6652-6657
    • Raghunathan, S.1    Ricard, C.S.2    Lohman, T.M.3    Waksman, G.4
  • 17
    • 0031567573 scopus 로고    scopus 로고
    • A common core for binding single-stranded DNA: Structural comparison of the single-stranded DNA-binding proteins (SSB) from E.coli and human mitochondria
    • [published errata appear in FEBS Lett October 6, 1997; 415(3):351 and October 27, 1997;416(3):387]
    • Webster,G., Genschel,J., Curth,U., Urbanke,C., Kang,C. and Hilgenfeld,R. (1997) A common core for binding single-stranded DNA: Structural comparison of the single-stranded DNA-binding proteins (SSB) from E.coli and human mitochondria [published errata appear in FEBS Lett October 6, 1997; 415(3):351 and October 27, 1997;416(3):387]. FEBS Lett., 411, 313-316.
    • (1997) FEBS Lett. , vol.411 , pp. 313-316
    • Webster, G.1    Genschel, J.2    Curth, U.3    Urbanke, C.4    Kang, C.5    Hilgenfeld, R.6
  • 18
    • 0041347886 scopus 로고    scopus 로고
    • Structure of Mycobacterium tuberculosis single-stranded DNA-binding protein. Variability in quaternary structure and its implications
    • Saikrishnan,K., Jeyakanthan,J., Venkatesh,J., Acharya,N., Sekar,K., Varshney,U. and Vijayan,M. (2003) Structure of Mycobacterium tuberculosis single-stranded DNA-binding protein. Variability in quaternary structure and its implications. J. Mol. Biol., 331, 385-393.
    • (2003) J. Mol. Biol. , vol.331 , pp. 385-393
    • Saikrishnan, K.1    Jeyakanthan, J.2    Venkatesh, J.3    Acharya, N.4    Sekar, K.5    Varshney, U.6    Vijayan, M.7
  • 19
    • 25144522675 scopus 로고    scopus 로고
    • Structure of Mycobacterium smegmatis single-stranded DNA-binding protein and a comparative study involving homologous SSBs: Biological implications of structural plasticity and variability in quaternary association
    • Saikrishnan,K., Manjunath,G.P., Singh,P., Jeyakanthan,J., Dauter,Z., Sekar,K., Muniyappa,K. and Vijayan,M. (2005) Structure of Mycobacterium smegmatis single-stranded DNA-binding protein and a comparative study involving homologous SSBs: Biological implications of structural plasticity and variability in quaternary association. Acta Crystallogr., Sect. D: Biol. Crystallogr., 61, 1140-1148.
    • (2005) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.61 , pp. 1140-1148
    • Saikrishnan, K.1    Manjunath, G.P.2    Singh, P.3    Jeyakanthan, J.4    Dauter, Z.5    Sekar, K.6    Muniyappa, K.7    Vijayan, M.8
  • 21
    • 0030014904 scopus 로고    scopus 로고
    • In vitro and in vivo function of the C-terminus of Escherichia coli single-stranded DNA binding protein
    • Curth,U., Genschel,J., Urbanke,C. and Greipel,J. (1996) In vitro and in vivo function of the C-terminus of Escherichia coli single-stranded DNA binding protein. Nucleic Acids Res., 24, 2706-2711.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2706-2711
    • Curth, U.1    Genschel, J.2    Urbanke, C.3    Greipel, J.4
  • 22
    • 1642521025 scopus 로고    scopus 로고
    • Crystal structure of the chi: psi subassembly of the Escherichia coli DNA polymerase clamp-loader complex
    • Gulbis,J.M., Kazmirski,S.L., Finkelstein,J., Kelman,Z., O'Donnell,M. and Kuriyan,J. (2004) Crystal structure of the chi: psi subassembly of the Escherichia coli DNA polymerase clamp-loader complex. Eur. J. Biochem., 271, 439-449.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 439-449
    • Gulbis, J.M.1    Kazmirski, S.L.2    Finkelstein, J.3    Kelman, Z.4    O'Donnell, M.5    Kuriyan, J.6
  • 23
    • 0015527130 scopus 로고
    • Affinity chromatography of phosphofructokinase using cibachrome blue F36-A
    • Böhme,H.J., Kopperschlägel,G., Schulz,J. and Hofmann,E. (1972) Affinity chromatography of phosphofructokinase using cibachrome blue F36-A. J. Chromat., 69, 209-214.
    • (1972) J. Chromat. , vol.69 , pp. 209-214
    • Böhme, H.J.1    Kopperschlägel, G.2    Schulz, J.3    Hofmann, E.4
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli,U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch,W. (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr., 26, 795-800.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 29
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones,T.A., Zou,J.-Y., Cowan,S.W. and Kjeldgaard,M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr., Sect. A: Found. Crystallogr., 47, 110-119.
    • (1991) Acta Crystallogr., Sect. A: Found. Crystallogr. , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 33
    • 0030498233 scopus 로고    scopus 로고
    • xdlMAPMAN and xdlDATAMAN-programmes for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflection data sets
    • Kleywegt,G.J. and Jones,T.A. (1996) xdlMAPMAN and xdlDATAMAN-programmes for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflection data sets. Acta Crystallogr.,Sect. D: Biol. Crystallogr., 52, 826-828.
    • (1996) Acta Crystallogr.,Sect. D: Biol. Crystallogr. , vol.52 , pp. 826-828
    • Kleywegt, G.J.1    Jones, T.A.2
  • 35
    • 0021216947 scopus 로고
    • Characterization of the structural and functional defect in the E.coli single-stranded DNA binding protein encoded by the ssb1 gene
    • Williams,K.R., Murphy,J.B. and Chase,J.W. (1984) Characterization of the structural and functional defect in the E.coli single-stranded DNA binding protein encoded by the ssb1 gene. J. Biol. Chem., 259, 11804-11811.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11804-11811
    • Williams, K.R.1    Murphy, J.B.2    Chase, J.W.3
  • 36
    • 0026064009 scopus 로고
    • Amino acid 55 plays a central role in tetramerization and function of Escherichia coli single-stranded DNA binding protein
    • Curth,U., Bayer,I., Greipel,J., Mayer,F., Urbanke,C. and Maass,G. (1991) Amino acid 55 plays a central role in tetramerization and function of Escherichia coli single-stranded DNA binding protein. Eur. J. Biochem., 196, 87-93.
    • (1991) Eur. J. Biochem. , vol.196 , pp. 87-93
    • Curth, U.1    Bayer, I.2    Greipel, J.3    Mayer, F.4    Urbanke, C.5    Maass, G.6
  • 37
    • 0141596172 scopus 로고    scopus 로고
    • Structural and functional adaptations to extreme temperatures in psychrophilic, Mesophilic, and Thermophilic DNA Ligases
    • Georlette,D., Damien,B., Blaise,V., Depiereux,E., Uversky,V.N., Gerday,C. and Feller,G. (2003) Structural and functional adaptations to extreme temperatures in psychrophilic, Mesophilic, and Thermophilic DNA Ligases. J. Biol. Chem., 278, 37015-37023.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37015-37023
    • Georlette, D.1    Damien, B.2    Blaise, V.3    Depiereux, E.4    Uversky, V.N.5    Gerday, C.6    Feller, G.7
  • 40
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones,G., Willett,P., Glen,R.C., Leach,A.R. and Taylor,R. (1997) Development and validation of a genetic algorithm for flexible docking. J. Mol. Biol., 267, 727-748.
    • (1997) J. Mol. Biol. , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 41
    • 0021345031 scopus 로고
    • Characterization of the E.coli ssb113 mutant single-stranded DNA binding protein. Cloning of the gene, DNA and protein sequence analysis, HPLC, peptide mapping and DNA binding studies
    • Chase,J.W., L'Italien,J.J., Murphy,J.B., Spicer,E.K. and Williams,K.R. (1984) Characterization of the E.coli ssb113 mutant single-stranded DNA binding protein. Cloning of the gene, DNA and protein sequence analysis, HPLC, peptide mapping and DNA binding studies. J. Biol. Chem., 259, 805-814.
    • (1984) J. Biol. Chem. , vol.259 , pp. 805-814
    • Chase, J.W.1    L'Italien, J.J.2    Murphy, J.B.3    Spicer, E.K.4    Williams, K.R.5
  • 42
    • 0018955332 scopus 로고
    • Effect of ssbA1 and lexC113 mutations on lambda prophage induction, bacteriophage growth, and cell survival
    • Vales,L.D., Chase,J.W. and Murphy,J.B. (1980) Effect of ssbA1 and lexC113 mutations on lambda prophage induction, bacteriophage growth, and cell survival. J Bacteriol., 143, 887-896.
    • (1980) J Bacteriol. , vol.143 , pp. 887-896
    • Vales, L.D.1    Chase, J.W.2    Murphy, J.B.3
  • 45
    • 0023644998 scopus 로고
    • Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 Å
    • Leijonmarck,M. and Liljas,A. (1987) Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 Å. J. Mol. Biol., 195, 555-579.
    • (1987) J. Mol. Biol. , vol.195 , pp. 555-579
    • Leijonmarck, M.1    Liljas, A.2
  • 46
    • 0020437699 scopus 로고
    • Structural studies of ribosomes
    • Liljas,A. (1982) Structural studies of ribosomes. Progr. Biophys. Mol. Biol., 40, 161-228.
    • (1982) Progr. Biophys. Mol. Biol. , vol.40 , pp. 161-228
    • Liljas, A.1


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