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Volumn 378, Issue 6, 1997, Pages 545-551

Overproduction of Sac7d and Sac7e reveals only Sac7e to be a DNA-Binding protein with ribonuclease activity from the extremophilic archaeon Sulfolobus acidocaldarius

Author keywords

Archaea; DNA binding proteins; Sulfolobus; Thermostable ribonuclease

Indexed keywords

BACTERIAL DNA; BACTERIAL ENZYME; BACTERIAL PROTEIN; BASIC PROTEIN; DNA BINDING PROTEIN; MESSENGER RNA; POLYCLONAL ANTIBODY; RECOMBINANT PROTEIN; RIBONUCLEASE;

EID: 0343852964     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/bchm.1997.378.6.545     Document Type: Article
Times cited : (8)

References (36)
  • 1
    • 0028322250 scopus 로고
    • Extended kinetic analysis of ribonuclease T1 variants leads to an improved scheme for the reaction mechanism
    • Backmann, J., Doray, C.C., Grunert, H.P., Landt, O., and Hahn, U. (1994). Extended kinetic analysis of ribonuclease T1 variants leads to an improved scheme for the reaction mechanism. Biochem. Biophys. Res. Commun. 199, 213-219.
    • (1994) Biochem. Biophys. Res. Commun. , vol.199 , pp. 213-219
    • Backmann, J.1    Doray, C.C.2    Grunert, H.P.3    Landt, O.4    Hahn, U.5
  • 2
    • 0028911769 scopus 로고
    • DNA-binding surface of the Sso7d protein from Sulfolobus solfataricus
    • Baumann, H., Knapp, S., Karshikoff, A., Ladenstein, R., and Härd, T. (1995). DNA-binding surface of the Sso7d protein from Sulfolobus solfataricus. J. Mol. Biol. 247, 840-846.
    • (1995) J. Mol. Biol. , vol.247 , pp. 840-846
    • Baumann, H.1    Knapp, S.2    Karshikoff, A.3    Ladenstein, R.4    Härd, T.5
  • 3
    • 0028533719 scopus 로고
    • Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus
    • Baumann, H., Knapp, S., Lundbäck, T., Ladenstein, R., and Härd, T. (1994). Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus. Struct. Biol. 1, 808-819.
    • (1994) Struct. Biol. , vol.1 , pp. 808-819
    • Baumann, H.1    Knapp, S.2    Lundbäck, T.3    Ladenstein, R.4    Härd, T.5
  • 4
    • 0019551730 scopus 로고
    • "Western Blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
    • Burnette, N.W. (1981). "Western Blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112, 195-203.
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, N.W.1
  • 5
    • 0023759962 scopus 로고
    • Isolation, characterization and microsequence analysis of a small basic methylated DNA-binding protein from the Archaebacterium, Sulfolobus solfataricus
    • Choli, T., Henning, P., Wittmann-Liebold, B., and Reinhardt, R. (1988a). Isolation, characterization and microsequence analysis of a small basic methylated DNA-binding protein from the Archaebacterium, Sulfolobus solfataricus. Biochim. Biophys. Acta 950, 193-203.
    • (1988) Biochim. Biophys. Acta , vol.950 , pp. 193-203
    • Choli, T.1    Henning, P.2    Wittmann-Liebold, B.3    Reinhardt, R.4
  • 6
    • 0023921980 scopus 로고
    • Microsequence analysis of DNA-binding proteins 7a, 7b, and 7e from the archaebacterium, Sulfolobus acidocaldarius
    • Choli, T., Wittmann-Liebold, B., and Reinhardt, R. (1988b). Microsequence analysis of DNA-binding proteins 7a, 7b, and 7e from the archaebacterium, Sulfolobus acidocaldarius. J. Biol. Chem. 263, 7087-7093.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7087-7093
    • Choli, T.1    Wittmann-Liebold, B.2    Reinhardt, R.3
  • 7
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomcynski, P., and Sacchi, N. (1987). Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomcynski, P.1    Sacchi, N.2
  • 8
    • 0003082897 scopus 로고
    • The structure of DNA-binding proteins from Eu- And Archaebacteria
    • K.O. Stetter and W. Zillig, eds. (Berlin: Springer Verlag)
    • Dijk, and Reinhardt, R. (1986). The structure of DNA-binding proteins from Eu-and Archaebacteria. In: Bacterial Chromatin, K.O. Stetter and W. Zillig, eds. (Berlin: Springer Verlag), pp. 185-218.
    • (1986) Bacterial Chromatin , pp. 185-218
    • Dijk1    Reinhardt, R.2
  • 9
    • 0028839434 scopus 로고
    • Solution structure of the DNA-binding protein Sac7d from the hyperthermophile Sulfolobus acidocaldarius
    • Edmondson, S.P., Qiu, L., and Shriver, J.W. (1995). Solution structure of the DNA-binding protein Sac7d from the hyperthermophile Sulfolobus acidocaldarius. Biochemistry 34, 13289-13304.
    • (1995) Biochemistry , vol.34 , pp. 13289-13304
    • Edmondson, S.P.1    Qiu, L.2    Shriver, J.W.3
  • 11
    • 0028967904 scopus 로고
    • In the thermophilic archaeon Sulfolobus solfataricus a DNA-binding protein is in vitro (ADPribosyl)ated
    • Faraone-Menella, M.R., and Farina, B. (1995). In the thermophilic archaeon Sulfolobus solfataricus a DNA-binding protein is in vitro (ADPribosyl)ated. Biochem. Biophys. Res. Commun. 208, 55-62.
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 55-62
    • Faraone-Menella, M.R.1    Farina, B.2
  • 12
    • 0029873327 scopus 로고    scopus 로고
    • 16S rDNA-based phylogeny of the archaeal order Sulfolobales and reclassification of Desulfurolobus ambivalens as Acidianus ambivalens comb. nov
    • Fuchs, T., Huber, H., Burggraf, S., and Stetter, K.O. (1996). 16S rDNA-based phylogeny of the archaeal order Sulfolobales and reclassification of Desulfurolobus ambivalens as Acidianus ambivalens comb. nov. System. App. Microbiol. 19, 56-60.
    • (1996) System. App. Microbiol. , vol.19 , pp. 56-60
    • Fuchs, T.1    Huber, H.2    Burggraf, S.3    Stetter, K.O.4
  • 14
    • 0028910484 scopus 로고
    • An 8.5-kDa ribonuclease from the extreme thermophilic archaebacterium Sulfolobus solfataricus
    • Fusi, P., Grisa, M., Tedeschi, G., Negri, A., Guerritore, A., and Tortora, P. (1995). An 8.5-kDa ribonuclease from the extreme thermophilic archaebacterium Sulfolobus solfataricus. FEBS Lett. 360, 187-190.
    • (1995) FEBS Lett. , vol.360 , pp. 187-190
    • Fusi, P.1    Grisa, M.2    Tedeschi, G.3    Negri, A.4    Guerritore, A.5    Tortora, P.6
  • 15
    • 0021017817 scopus 로고
    • Histone-like protein in the archaebacterium Sulfolobus acidocaldarius
    • Green, G.R., Saercy, D.G., and DeLange, R.J. (1983). Histone-like protein in the archaebacterium Sulfolobus acidocaldarius. Biochim. Biophys. Acta. 741, 251-257.
    • (1983) Biochim. Biophys. Acta. , vol.741 , pp. 251-257
    • Green, G.R.1    Saercy, D.G.2    Delange, R.J.3
  • 16
    • 0022478821 scopus 로고
    • Ribosomal and DNA binding proteins of the thermoacidophilic archaebactenum Sulfolobus acidocaldarius
    • Grote, M., Dijk, J., and Reinhardt, R. (1986). Ribosomal and DNA binding proteins of the thermoacidophilic archaebactenum Sulfolobus acidocaldarius. Biochim. Biophys. Acta. 873, 405-413.
    • (1986) Biochim. Biophys. Acta. , vol.873 , pp. 405-413
    • Grote, M.1    Dijk, J.2    Reinhardt, R.3
  • 17
    • 0023753102 scopus 로고
    • The use of polyvinylidenefluoride membranes as a general blotting matrix
    • Gültekin, H., and Heermann, K.H. (1988). The use of polyvinylidenefluoride membranes as a general blotting matrix. Anal. Biochem. 172, 320-329.
    • (1988) Anal. Biochem. , vol.172 , pp. 320-329
    • Gültekin, H.1    Heermann, K.H.2
  • 18
    • 0000298607 scopus 로고
    • Structure determination, modelling and site-directed mutagenesis studies of ribonuclease T1
    • P. Wrede and G. Schneider, eds. (Berlin & New York: Walter de Gruyter & Co.)
    • Hahn, U., and Heinemann, U. (1994). Structure determination, modelling and site-directed mutagenesis studies of ribonuclease T1. In: Concepts of Protein Engineering and Design, Vol. I, P. Wrede and G. Schneider, eds. (Berlin & New York: Walter de Gruyter & Co.), pp. 109-168.
    • (1994) Concepts of Protein Engineering and Design , vol.1 , pp. 109-168
    • Hahn, U.1    Heinemann, U.2
  • 20
    • 0021764377 scopus 로고
    • The amino acid sequence of a small DNa binding protein from the archaebacterium Sulfolobus acidocaldarius
    • Kimura, M., Kimura, J., Davie, P., Reinhardt, R., and Dijk, J. (1984). The amino acid sequence of a small DNA binding protein from the archaebacterium Sulfolobus acidocaldarius. FEBS Lett. 176, 176-178.
    • (1984) FEBS Lett. , vol.176 , pp. 176-178
    • Kimura, M.1    Kimura, J.2    Davie, P.3    Reinhardt, R.4    Dijk, J.5
  • 21
    • 0029095909 scopus 로고
    • SaRD, a new protein isolated from the extremophile archaeon Sulfolobus acidocaldarius, is a thermostable ribonuclease with DNA-binding properties
    • Kulms, D., Schäfer, G., and Hahn, U. (1995). SaRD, A new protein isolated from the extremophile archaeon Sulfolobus acidocaldarius, is a thermostable ribonuclease with DNA-binding properties. Biochem. Biophys. Res. Commun. 214, 646-652.
    • (1995) Biochem. Biophys. Res. Commun. , vol.214 , pp. 646-652
    • Kulms, D.1    Schäfer, G.2    Hahn, U.3
  • 22
    • 0001270373 scopus 로고
    • Electron microscopic study of DNA complexes with proteins from the Archaebacterium Sulfolobus acidocaldarius
    • Lurz, R., Grote, M., Dijk, J., Reinhardt, R., and Dobrinski, B. (1986). Electron microscopic study of DNA complexes with proteins from the Archaebacterium Sulfolobus acidocaldarius. EMBO J. 5, 3715-3721.
    • (1986) EMBO J. , vol.5 , pp. 3715-3721
    • Lurz, R.1    Grote, M.2    Dijk, J.3    Reinhardt, R.4    Dobrinski, B.5
  • 23
    • 85010439719 scopus 로고
    • A procedure for the isolation of desoxyribonucleic acid from microorganisms
    • Marmur, J. (1961). A procedure for the isolation of desoxyribonucleic acid from microorganisms. J. Mol. Biol. 3, 208-218.
    • (1961) J. Mol. Biol. , vol.3 , pp. 208-218
    • Marmur, J.1
  • 24
    • 0029156641 scopus 로고
    • Gene cloning, expression and characterization of the Sac7 proteins from the hyperthermophile Sulfolobus acidocaldarius
    • McAfee, J.G., Edmondson, S.P., Datta, P.K., Shriver, J.W., and Gupta, R. (1995). Gene cloning, expression and characterization of the Sac7 proteins from the hyperthermophile Sulfolobus acidocaldarius. Biochemistry 34, 10063-10077.
    • (1995) Biochemistry , vol.34 , pp. 10063-10077
    • McAfee, J.G.1    Edmondson, S.P.2    Datta, P.K.3    Shriver, J.W.4    Gupta, R.5
  • 25
    • 0027183545 scopus 로고
    • Ribozymes: A distinct class of metalloenzymes
    • Pyle, A.M. (1993). Ribozymes: a distinct class of metalloenzymes Science 261, 709-714.
    • (1993) Science , vol.261 , pp. 709-714
    • Pyle, A.M.1
  • 26
    • 0004854044 scopus 로고
    • Novel histone-like DNA-binding proteins in the nucleoid from the acidophilic archaebacterium Sulfolobus acidocaldarius that protect DNA against thermal denaturation
    • Reddy, T.R., and Suryanarayana, T. (1988). Novel histone-like DNA-binding proteins in the nucleoid from the acidophilic archaebacterium Sulfolobus acidocaldarius that protect DNA against thermal denaturation. Biochim. Biophys. Acta. 949, 87-96.
    • (1988) Biochim. Biophys. Acta. , vol.949 , pp. 87-96
    • Reddy, T.R.1    Suryanarayana, T.2
  • 27
    • 0024971515 scopus 로고
    • Archaebacterial histone-like proteins purification and characterization of helix stabilizing DNA binding proteins from the acidophile Sulfolobusacidocaldarius
    • Reddy, T.R., and Suryanarayana, T. (1989). Archaebacterial histone-like proteins purification and characterization of helix stabilizing DNA binding proteins from the acidophile Sulfolobusacidocaldarius. J. Biol. Chem. 264, 17298-17308.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17298-17308
    • Reddy, T.R.1    Suryanarayana, T.2
  • 29
    • 0025301592 scopus 로고
    • HMf, a DNA-binding protein isolated from the hyperthermophilic archaeon Methanothermus fervidus, is most closely related to histones
    • Sandman, K., Krzycki, A., Dobrinski, B., Lurz, R., and Reeve, J.N. (1990). HMf, a DNA-binding protein isolated from the hyperthermophilic archaeon Methanothermus fervidus, is most closely related to histones. Proc. Natl. Acad. Sci. USA 87, 5788-5791.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5788-5791
    • Sandman, K.1    Krzycki, A.2    Dobrinski, B.3    Lurz, R.4    Reeve, J.N.5
  • 30
    • 0026059558 scopus 로고
    • Nonradioactive labeling of oligonucleotides in vitro with the Hapten digoxygenin by tailing with terminal transferase
    • Schmitz, G.G., Walter, T., Seibl, R., and Kessler, C. (1991). Nonradioactive labeling of oligonucleotides in vitro with the Hapten digoxygenin by tailing with terminal transferase. Anal. Biochem. 192, 222-231.
    • (1991) Anal. Biochem. , vol.192 , pp. 222-231
    • Schmitz, G.G.1    Walter, T.2    Seibl, R.3    Kessler, C.4
  • 31
    • 0016832016 scopus 로고
    • Histone-like protein in the prokaryote Thermoplasma acidophilum
    • Searcy, D.G. (1975). Histone-like protein in the prokaryote Thermoplasma acidophilum. Biochim. Biophys. Acta 395, 535-547.
    • (1975) Biochim. Biophys. Acta , vol.395 , pp. 535-547
    • Searcy, D.G.1
  • 32
    • 0019333617 scopus 로고
    • Thermoplasma acidophilum histone-like protein: Partial amino acid sequence suggestive of homology to eukaryotic histones
    • Searcy, D.G., and DeLange, R.J. (1980). Thermoplasma acidophilum histone-like protein: Partial amino acid sequence suggestive of homology to eukaryotic histones. Biochim. Biophs. Acta 609, 197-200.
    • (1980) Biochim. Biophs. Acta , vol.609 , pp. 197-200
    • Searcy, D.G.1    DeLange, R.J.2
  • 33
    • 0019333622 scopus 로고
    • Nucleoprotein subunit structure in an unusual procaryotic organism: Thermoplasma acidophilum
    • Searcy, D.G., and Stein, D.B. (1980). Nucleoprotein subunit structure in an unusual procaryotic organism: Thermoplasma acidophilum. Biochim. Biophys. Acta 609, 180-195.
    • (1980) Biochim. Biophys. Acta , vol.609 , pp. 180-195
    • Searcy, D.G.1    Stein, D.B.2
  • 34
    • 0017957162 scopus 로고
    • Phylogenetic affinities between eucaryotic cells and a thermophilic mycoplasma
    • Searcy, D.G., Stein, D.B., and Green, G.R. (1978). Phylogenetic affinities between eucaryotic cells and a thermophilic mycoplasma. Biosystems 10, 19-28.
    • (1978) Biosystems , vol.10 , pp. 19-28
    • Searcy, D.G.1    Stein, D.B.2    Green, G.R.3
  • 35
    • 0018182105 scopus 로고
    • Physiologically important stabilization of DNa by a procaryotic histone-like protein
    • Stein, D.B., and Searcy, D.G. (1978). Physiologically important stabilization of DNA by a procaryotic histone-like protein. Science 202, 219-221.
    • (1978) Science , vol.202 , pp. 219-221
    • Stein, D.B.1    Searcy, D.G.2
  • 36
    • 0027953901 scopus 로고
    • Structural characterization of a three-disulfide intermediate of ribonuclease a involved in both the folding and unfolding pathways
    • Talluri, S., Rothwarf, D.M., and Scheraga, H.A. (1994). Structural characterization of a three-disulfide intermediate of ribonuclease A involved in both the folding and unfolding pathways. Biochemistry 33, 10437-10449.
    • (1994) Biochemistry , vol.33 , pp. 10437-10449
    • Talluri, S.1    Rothwarf, D.M.2    Scheraga, H.A.3


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