메뉴 건너뛰기




Volumn 267, Issue 4, 1997, Pages 841-848

Annealing of complementary DNA strands above the melting point of the duplex promoted by an archaeal protein

Author keywords

Archaea; DNA annealing; DNA binding protein; Homologous pairing; Thermophiles

Indexed keywords

BACTERIAL DNA; COMPLEMENTARY DNA; DNA BINDING PROTEIN; DOUBLE STRANDED DNA; NUCLEIC ACID;

EID: 0031564652     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0873     Document Type: Article
Times cited : (43)

References (38)
  • 1
    • 0027192062 scopus 로고
    • Nucleotide sequence of a gene encoding a histone-like protein in the archaeon Methanococcus voltae
    • Agha-Amiri K., Klein A. Nucleotide sequence of a gene encoding a histone-like protein in the archaeon Methanococcus voltae. Nucl. Acids Res. 21:1993;1491.
    • (1993) Nucl. Acids Res. , vol.21 , pp. 1491
    • Agha-Amiri, K.1    Klein, A.2
  • 2
    • 0014963741 scopus 로고
    • T4 bacteriophage gene 32: A structural protein in the replication and recombination of DNA
    • Alberts B. M., Frey L. T4 bacteriophage gene 32: a structural protein in the replication and recombination of DNA. Nature. 227:1970;1313-1317.
    • (1970) Nature , vol.227 , pp. 1313-1317
    • Alberts, B.M.1    Frey, L.2
  • 3
    • 0028533719 scopus 로고
    • Solution structure and DNA-binding properties of a small thermostable protein from the Archaeon Sulfolobus solfataricus
    • Baumann H., Knapp S., Lundback T., Ladenstein R., Hard T. Solution structure and DNA-binding properties of a small thermostable protein from the Archaeon Sulfolobus solfataricus. Nature Struct. Biol. 1:1994;808-819.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 808-819
    • Baumann, H.1    Knapp, S.2    Lundback, T.3    Ladenstein, R.4    Hard, T.5
  • 4
    • 0028911769 scopus 로고
    • DNA-binding surface of the Sso7d protein from Sulfolobus solfataricus
    • Baumann H., Knapp S., Karshikoff A., Ladenstein R., Hard T. DNA-binding surface of the Sso7d protein from Sulfolobus solfataricus. J. Mol. Biol. 247:1995;840-846.
    • (1995) J. Mol. Biol. , vol.247 , pp. 840-846
    • Baumann, H.1    Knapp, S.2    Karshikoff, A.3    Ladenstein, R.4    Hard, T.5
  • 5
    • 0026019440 scopus 로고
    • HU and IHF, two homologous histone-like proteins of Escherichia coli, form different protein-DNA complexes with short DNA fragments
    • Bonnefoy E., Rouviere-Yaniv J. HU and IHF, two homologous histone-like proteins of Escherichia coli, form different protein-DNA complexes with short DNA fragments. EMBO J. 10:1991;687-696.
    • (1991) EMBO J. , vol.10 , pp. 687-696
    • Bonnefoy, E.1    Rouviere-Yaniv, J.2
  • 6
    • 0021910631 scopus 로고
    • On the mechanism of renaturation of complementary DNA strands by the recA protein of Escherichia coli
    • Bryant F. R., Lehman I. R. On the mechanism of renaturation of complementary DNA strands by the recA protein of Escherichia coli. Proc. Natl Acad. Sci. USA. 82:1985;297-301.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 297-301
    • Bryant, F.R.1    Lehman, I.R.2
  • 7
    • 0024595909 scopus 로고
    • Kinetic modeling of the RecA protein promoted renaturation of complementary DNA strands
    • Bryant F. R., Menge K. L., Nguyen T. T. Kinetic modeling of the RecA protein promoted renaturation of complementary DNA strands. Biochemistry. 28:1989;1062-1069.
    • (1989) Biochemistry , vol.28 , pp. 1062-1069
    • Bryant, F.R.1    Menge, K.L.2    Nguyen, T.T.3
  • 8
    • 0024969026 scopus 로고
    • Primary structure of the chromosomal protein MC1 from the archaebacterium Methanosarcina sp. CHTI 55
    • Chartier F., Laine B., Belaiche D., Touzel J. P., Sautiere P. Primary structure of the chromosomal protein MC1 from the archaebacterium Methanosarcina sp. CHTI 55. Biochim. Biophys. Acta. 1008:1989;309-314.
    • (1989) Biochim. Biophys. Acta , vol.1008 , pp. 309-314
    • Chartier, F.1    Laine, B.2    Belaiche, D.3    Touzel, J.P.4    Sautiere, P.5
  • 9
    • 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., Reinhardt R. Isolation, characterization and microsequence analysis of a small basic methylated DNA-binding protein from the Archaebacterium, Sulfolobus solfataricus. Biochim. Biophys. Acta. 950:1988a;193-203.
    • (1988) Biochim. Biophys. Acta , vol.950 , pp. 193-203
    • Choli, T.1    Henning, P.2    Wittmann-Liebold, B.3    Reinhardt, R.4
  • 10
    • 0023921980 scopus 로고
    • Microsequence analysis of DNA-binding proteins 7a, 7b, and 7e from the archaebacterium Sulfolobus acidocaldarius
    • Choli T., Wittmann-Liebold B., Reinhardt R. Microsequence analysis of DNA-binding proteins 7a, 7b, and 7e from the archaebacterium Sulfolobus acidocaldarius. J. Biol. Chem. 263:1988b;7087-7093.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7087-7093
    • Choli, T.1    Wittmann-Liebold, B.2    Reinhardt, R.3
  • 11
    • 0027217660 scopus 로고
    • Phosphorylation of human hnRNP protein A1 abrogates in vitro strand annealing activity
    • Cobianchi F., Calvio C., Stoppini M., Buvoli M., Riva S. Phosphorylation of human hnRNP protein A1 abrogates in vitro strand annealing activity. Nucl. Acids Res. 21:1993;949-955.
    • (1993) Nucl. Acids Res. , vol.21 , pp. 949-955
    • Cobianchi, F.1    Calvio, C.2    Stoppini, M.3    Buvoli, M.4    Riva, S.5
  • 12
    • 0025010855 scopus 로고
    • Isolation and sequencing of a new beta-galactosidase-encoding archaebacterial gene
    • Cubellis M. V., Rozzo C., Montecucchi P., Rossi M. Isolation and sequencing of a new beta-galactosidase-encoding archaebacterial gene. Gene. 94:1990;89-94.
    • (1990) Gene , vol.94 , pp. 89-94
    • Cubellis, M.V.1    Rozzo, C.2    Montecucchi, P.3    Rossi, M.4
  • 13
    • 0026628854 scopus 로고
    • Viral RNA annealing activities of human immunodeficiency virus type 1 nucleocapsid protein require only peptide domains outside the zinc fingers
    • De Rocquigny H., Gabus C., Vincent A., Fournié-Zaluski M.-C., Roques B., Darlix J.-L. Viral RNA annealing activities of human immunodeficiency virus type 1 nucleocapsid protein require only peptide domains outside the zinc fingers. Proc. Natl Acad. Sci. USA. 89:1992;6472-6476.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 6472-6476
    • De Rocquigny, H.1    Gabus, C.2    Vincent, A.3    Fournié-Zaluski, M.-C.4    Roques, B.5    Darlix, J.-L.6
  • 14
    • 0029928176 scopus 로고    scopus 로고
    • Ku86 defines genetic defect and restores X-ray resistance and V(D)J recombination to complementation group 5 hamster cell mutants
    • Errami A., Smider V., Rathmell W. K., He D. M., Hendrickson E. A., Zdzienicka M. Z., Chu G. Ku86 defines genetic defect and restores X-ray resistance and V(D)J recombination to complementation group 5 hamster cell mutants. Mol. Cell Biol. 16:1996;1519-1526.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 1519-1526
    • Errami, A.1    Smider, V.2    Rathmell, W.K.3    He, D.M.4    Hendrickson, E.A.5    Zdzienicka, M.Z.6    Chu, G.7
  • 16
    • 0021017817 scopus 로고
    • Histone-like protein in the Archaebacterium Sulfolobus acidocaldarius
    • Green G. R., Searcy D. G., DeLange R. J. Histone-like protein in the Archaebacterium Sulfolobus acidocaldarius. Biochim. Biophys. Acta. 741:1983;251-257.
    • (1983) Biochim. Biophys. Acta , vol.741 , pp. 251-257
    • Green, G.R.1    Searcy, D.G.2    Delange, R.J.3
  • 17
    • 0026538880 scopus 로고
    • Isolation of a thermostable enzyme catalyzing disulfide bond formation from the archaebacterium Sulfolobus solfataricus
    • Guagliardi A., Cerchia L., De Rosa M., Rossi M., Bartolucci S. Isolation of a thermostable enzyme catalyzing disulfide bond formation from the archaebacterium Sulfolobus solfataricus. FEBS Letters. 303:1992;27-30.
    • (1992) FEBS Letters , vol.303 , pp. 27-30
    • Guagliardi, A.1    Cerchia, L.2    De Rosa, M.3    Rossi, M.4    Bartolucci, S.5
  • 18
    • 0000543393 scopus 로고
    • DBF (disulfide bond forming) enzyme from the hyperthermophilic archaebacterium Sulfolobus solfataricus behaves like a molecular chaperone
    • Guagliardi A., Cerchia L., Camardella L., Rossi M., Bartolucci S. DBF (disulfide bond forming) enzyme from the hyperthermophilic archaebacterium Sulfolobus solfataricus behaves like a molecular chaperone. Biocatalysis. 11:1994;181-190.
    • (1994) Biocatalysis , vol.11 , pp. 181-190
    • Guagliardi, A.1    Cerchia, L.2    Camardella, L.3    Rossi, M.4    Bartolucci, S.5
  • 19
  • 21
    • 0021764377 scopus 로고
    • The amino acid sequence of a small DNA binding protein from the Archaebacterium Sulfolobus solfataricus
    • Kimura M., Kimura J., Davie P., Reinhardt R., Dijk J. The amino acid sequence of a small DNA binding protein from the Archaebacterium Sulfolobus solfataricus. FEBS Letters. 176:1984;176-178.
    • (1984) FEBS Letters , vol.176 , pp. 176-178
    • Kimura, M.1    Kimura, J.2    Davie, P.3    Reinhardt, R.4    Dijk, J.5
  • 22
    • 0028308710 scopus 로고
    • Homologous pairing and DNA strand-exchange proteins
    • Kowalczykowski S. C., Eggelston A. K. Homologous pairing and DNA strand-exchange proteins. Annu. Rev. Biochem. 63:1994;991-1043.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 991-1043
    • Kowalczykowski, S.C.1    Eggelston, A.K.2
  • 23
    • 0028236899 scopus 로고
    • DNA stability at temperatures typical for hyperthermophiles
    • Marguet E., Forterre P. DNA stability at temperatures typical for hyperthermophiles. Nucl. Acids Res. 22:1994;1681-1686.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 1681-1686
    • Marguet, E.1    Forterre, P.2
  • 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., Gupta R. Gene cloning, expression, and characterization of the Sac7 proteins from the hyperthermophile Sulfolobus acidocaldarius. Biochemistry. 34:1995;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
    • 0346660225 scopus 로고
    • Initiation of general recombination calatyzed in vitro by the RecA protein of Escherichia coli
    • McEntee K., Weinstock G. M., Lehman I. R. Initiation of general recombination calatyzed in vitro by the RecA protein of Escherichia coli. Proc. Natl Acad. Sci. USA. 76:1979;2615-2619.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 2615-2619
    • McEntee, K.1    Weinstock, G.M.2    Lehman, I.R.3
  • 26
    • 0026542466 scopus 로고
    • Heterogeneous nuclear ribonucleoprotein A1 catalyzes RNA-RNA annealing
    • Munroe S. H., Dong X. Heterogeneous nuclear ribonucleoprotein A1 catalyzes RNA-RNA annealing. Proc. Natl Acad. Sci. USA. 89:1992;895-899.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 895-899
    • Munroe, S.H.1    Dong, X.2
  • 27
    • 0025885691 scopus 로고
    • DNA binding by the archaeal histone HMf results in positive supercoiling
    • Musgrave D. R., Sandman K. M., Reeve J. N. DNA binding by the archaeal histone HMf results in positive supercoiling. Proc. Natl Acad. Sci. USA. 88:1991;10397-10401.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 10397-10401
    • Musgrave, D.R.1    Sandman, K.M.2    Reeve, J.N.3
  • 28
    • 0027284915 scopus 로고
    • P-53 catalyzed annealing of complementary single stranded nucleic acids
    • Oberosler P., Hloch P., Ramsperger U., Stahl H. p-53 catalyzed annealing of complementary single stranded nucleic acids. EMBO J. 12:1993;2389-2396.
    • (1993) EMBO J. , vol.12 , pp. 2389-2396
    • Oberosler, P.1    Hloch, P.2    Ramsperger, U.3    Stahl, H.4
  • 29
    • 0024971515 scopus 로고
    • Archaebacterial histone-like proteins
    • Reddy T. R., Suryanarayana T. Archaebacterial histone-like proteins. J. Biol. Chem. 264:1989;17298-17308.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17298-17308
    • Reddy, T.R.1    Suryanarayana, T.2
  • 31
    • 0025301592 scopus 로고
    • HMf, a DNA-binding protein isolated from the hyperthermophilic archaeon Methanothermus fervidus, is most closely related to histones
    • Sandman K., Krzycki J. A., Dobrinski B., Lurz R., Reeve J. N. HMf, a DNA-binding protein isolated from the hyperthermophilic archaeon Methanothermus fervidus, is most closely related to histones. Proc. Natl Acad. Sci. USA. 87:1990;5788-5791.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 5788-5791
    • Sandman, K.1    Krzycki, J.A.2    Dobrinski, B.3    Lurz, R.4    Reeve, J.N.5
  • 32
    • 0004867938 scopus 로고
    • The archaebacterial histone HTa
    • Heidelberg: Springer-Verlag
    • Searcy D. G. The archaebacterial histone HTa. Bacterial Chromatin. 1986;Springer-Verlag, Heidelberg.
    • (1986) Bacterial Chromatin
    • Searcy, D.G.1
  • 33
    • 0026345115 scopus 로고
    • Complementary recognition in condensed DNA: Accelerated DNA renaturation
    • Sikorav J.-L., Church G. M. Complementary recognition in condensed DNA: accelerated DNA renaturation. J. Mol. Biol. 222:1991;1085-1108.
    • (1991) J. Mol. Biol. , vol.222 , pp. 1085-1108
    • Sikorav, J.-L.1    Church, G.M.2
  • 34
    • 0027978039 scopus 로고
    • Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast RAD51 protein
    • Sung P. Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast RAD51 protein. Science. 265:1994;1241-1243.
    • (1994) Science , vol.265 , pp. 1241-1243
    • Sung, P.1
  • 35
    • 0026557114 scopus 로고
    • Renaturation of DNA catalysed by yeast DNA repair and recombination protein RAD10
    • Sung P., Prakash L. A., Prakash S. Renaturation of DNA catalysed by yeast DNA repair and recombination protein RAD10. Nature. 355:1992;743-745.
    • (1992) Nature , vol.355 , pp. 743-745
    • Sung, P.1    Prakash, L.A.2    Prakash, S.3
  • 36
    • 0028226799 scopus 로고
    • DNA chaperones: A solution to a persistence problem
    • Travers A. A., Ner S. S., Churchill M. E. A. DNA chaperones: a solution to a persistence problem. Cell. 77:1994;167-169.
    • (1994) Cell , vol.77 , pp. 167-169
    • Travers, A.A.1    Ner, S.S.2    Churchill, M.E.A.3
  • 37
    • 0028129970 scopus 로고
    • DNA strand exchange and selective DNA annealing promoted by the Human Imunodeficiency Virus Type I nucleocapsid protein
    • Tsuchihashi Z., Brown P. O. DNA strand exchange and selective DNA annealing promoted by the Human Imunodeficiency Virus Type I nucleocapsid protein. J.Virol. 68:1994;5863-5970.
    • (1994) J.Virol. , vol.68 , pp. 5863-5970
    • Tsuchihashi, Z.1    Brown, P.O.2
  • 38
    • 0344734266 scopus 로고
    • ATP-dependent renaturation of DNA catalyzed by the recA protein of Escherichia coli
    • Weinstock G. M., McEntee K., Lehman I. R. ATP-dependent renaturation of DNA catalyzed by the recA protein of Escherichia coli. Proc. Natl. Acad. Sci. USA. 76:1979;126-130.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 126-130
    • Weinstock, G.M.1    McEntee, K.2    Lehman, I.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.