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Volumn 224, Issue 1, 2003, Pages 17-22

Surface histidine residue of archaeal histone affects DNA compaction and thermostability

Author keywords

Compaction; Histone; Hyperthermophile; KOD1; Mutation; Tetramer; Thermococcus kodakaraensis

Indexed keywords

ALANINE; DNA; FUNGAL PROTEIN; GLYCINE; HISTIDINE; HISTONE; MUTANT PROTEIN; PROTEIN HPKB; PROTEIN KOD1; UNCLASSIFIED DRUG; VALINE;

EID: 0038647127     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(03)00358-6     Document Type: Article
Times cited : (4)

References (20)
  • 1
    • 0027431478 scopus 로고
    • Topography of the histone octamer surface: Repeating structural motifs utilized in the docking of nucleosomal DNA
    • Arents G., Moudrianakis E.N. Topography of the histone octamer surface: Repeating structural motifs utilized in the docking of nucleosomal DNA. Proc. Natl. Acad. Sci. USA. 90:1993;10489-10493.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10489-10493
    • Arents, G.1    Moudrianakis, E.N.2
  • 2
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger K., Mäder A.W., Richmond R.K., Sargent D.F., Richmond T.J. Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature. 389:1997;251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mäder, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 4
    • 0036307707 scopus 로고    scopus 로고
    • Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 Å resolution
    • Davey C.A., Sargent D.F., Luger K., Maeder A.W., Richmond T.J. Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 Å resolution. J. Mol. Biol. 319:2002;1097-1113.
    • (2002) J. Mol. Biol. , vol.319 , pp. 1097-1113
    • Davey, C.A.1    Sargent, D.F.2    Luger, K.3    Maeder, A.W.4    Richmond, T.J.5
  • 5
    • 0032144071 scopus 로고    scopus 로고
    • Histones and nucleosomes in Archaea and Eukarya: A comparative analysis
    • Pereira S.L., Reeve J.N. Histones and nucleosomes in Archaea and Eukarya: a comparative analysis. Extremophiles. 2:1998;141-148.
    • (1998) Extremophiles , vol.2 , pp. 141-148
    • Pereira, S.L.1    Reeve, J.N.2
  • 6
    • 0029924193 scopus 로고    scopus 로고
    • NMR structure of HMfB from the hyperthermophile, Methanothermus fervidus, confirms that this archaeal protein is a histone
    • Starich M.R., Sandman K., Reeve J.N., Summers M.F. NMR structure of HMfB from the hyperthermophile, Methanothermus fervidus, confirms that this archaeal protein is a histone. J. Mol. Biol. 255:1996;187-203.
    • (1996) J. Mol. Biol. , vol.255 , pp. 187-203
    • Starich, M.R.1    Sandman, K.2    Reeve, J.N.3    Summers, M.F.4
  • 7
    • 0029006334 scopus 로고
    • Structure and stability of histone HMf from the hyperthermophilic archaeon Methanothermus fervidus
    • Grayling R.A., Becktel W.J., Reeve J.N. Structure and stability of histone HMf from the hyperthermophilic archaeon Methanothermus fervidus. Biochemistry. 34:1995;8441-8448.
    • (1995) Biochemistry , vol.34 , pp. 8441-8448
    • Grayling, R.A.1    Becktel, W.J.2    Reeve, J.N.3
  • 10
    • 0033542121 scopus 로고    scopus 로고
    • Analysis of DNA compaction profile and intracellular contents of archaeal histones from Pyrococcus kodakaraensis KOD1
    • Higashibata H., Fujiwara S., Takagi M., Imanaka T. Analysis of DNA compaction profile and intracellular contents of archaeal histones from Pyrococcus kodakaraensis KOD1. Biochem. Biophys. Res. Commun. 258:1999;416-424.
    • (1999) Biochem. Biophys. Res. Commun. , vol.258 , pp. 416-424
    • Higashibata, H.1    Fujiwara, S.2    Takagi, M.3    Imanaka, T.4
  • 11
    • 0028130396 scopus 로고
    • Histone-encoding genes from Pyrococcus: Evidence for members of the HMf family of archaeal histones in a non-methanogenic Archaeon
    • Sandman K., Perler F.B., Reeve J.N. Histone-encoding genes from Pyrococcus: evidence for members of the HMf family of archaeal histones in a non-methanogenic Archaeon. Gene. 150:1994;207-208.
    • (1994) Gene , vol.150 , pp. 207-208
    • Sandman, K.1    Perler, F.B.2    Reeve, J.N.3
  • 12
    • 0026729921 scopus 로고
    • HMt, a histone-related protein from Methanobacterium thermoautotrophicum delta H
    • Tabassum R., Sandman K.M., Reeve J.N. HMt, a histone-related protein from Methanobacterium thermoautotrophicum delta H. J. Bacteriol. 174:1992;7890-7895.
    • (1992) J. Bacteriol. , vol.174 , pp. 7890-7895
    • Tabassum, R.1    Sandman, K.M.2    Reeve, J.N.3
  • 13
    • 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
  • 14
    • 0028930574 scopus 로고
    • Methanobacterium formicicum, a mesophilic methanogen, contains three HFo histones
    • Darcy T.J., Sandman K., Reeve J.N. Methanobacterium formicicum, a mesophilic methanogen, contains three HFo histones. J. Bacteriol. 177:1995;858-860.
    • (1995) J. Bacteriol. , vol.177 , pp. 858-860
    • Darcy, T.J.1    Sandman, K.2    Reeve, J.N.3
  • 15
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:1987;368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 16
    • 0030012909 scopus 로고    scopus 로고
    • Histones and chromatin structure in hyperthermophilic archaea
    • Grayling R.A., Sandman K., Reeve J.N. Histones and chromatin structure in hyperthermophilic archaea. FEMS Microbiol. Rev. 18:1996;203-213.
    • (1996) FEMS Microbiol. Rev. , vol.18 , pp. 203-213
    • Grayling, R.A.1    Sandman, K.2    Reeve, J.N.3
  • 18
    • 0034677666 scopus 로고    scopus 로고
    • Mutational analysis of archaeal histone-DNA interactions
    • Soares D.J., Sandman K., Reeve J.N. Mutational analysis of archaeal histone-DNA interactions. J. Mol. Biol. 297:2000;39-47.
    • (2000) J. Mol. Biol. , vol.297 , pp. 39-47
    • Soares, D.J.1    Sandman, K.2    Reeve, J.N.3
  • 19
    • 0033972056 scopus 로고    scopus 로고
    • Mutational analysis of differences in thermostability between histones from mesophilic and hyperthermophilic archaea
    • Li W.-T., Shriver J.W., Reeve J.N. Mutational analysis of differences in thermostability between histones from mesophilic and hyperthermophilic archaea. J. Bacteriol. 182:2000;812-817.
    • (2000) J. Bacteriol. , vol.182 , pp. 812-817
    • Li, W.-T.1    Shriver, J.W.2    Reeve, J.N.3
  • 20
    • 0037163112 scopus 로고    scopus 로고
    • Archaeal histone tetramerization determines DNA affinity and the direction of DNA supercoiling
    • Marc F., Sandman K., Lurz R., Reeve J.N. Archaeal histone tetramerization determines DNA affinity and the direction of DNA supercoiling. J. Biol. Chem. 277:2002;30879-30886.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30879-30886
    • Marc, F.1    Sandman, K.2    Lurz, R.3    Reeve, J.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.