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Volumn 14, Issue 12, 2003, Pages 4758-4769

Glom Is a Novel Mitochondrial DNA Packaging Protein in Physarum polycephalum and Causes Intense Chromatin Condensation without Suppressing DNA Functions

Author keywords

[No Author keywords available]

Indexed keywords

GLOM PROTEIN; HISTONE; HU PROTEIN; MITOCHONDRIAL DNA; MITOCHONDRIAL DNA PACKAGING PROTEIN; MITOCHONDRIAL PROTEIN; PROLINE; UNCLASSIFIED DRUG;

EID: 10744231984     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E03-02-0099     Document Type: Article
Times cited : (49)

References (69)
  • 2
    • 0022446807 scopus 로고
    • Roles of H1 domains in determining higher order chromatin structure and H1 location
    • Allan, J., Mitchell, T., Harborne, N., Bohm, L., and Crane-Robinson, C. (1986). Roles of H1 domains in determining higher order chromatin structure and H1 location. J. Mol. Biol. 187, 591-601.
    • (1986) J. Mol. Biol. , vol.187 , pp. 591-601
    • Allan, J.1    Mitchell, T.2    Harborne, N.3    Bohm, L.4    Crane-Robinson, C.5
  • 4
    • 0032512051 scopus 로고    scopus 로고
    • The genome sequence of Rickettsia prowazekii and the origin of mitochondria
    • Andersson, S.G. et al. (1998). The genome sequence of Rickettsia prowazekii and the origin of mitochondria. Nature 396, 133-140.
    • (1998) Nature , vol.396 , pp. 133-140
    • Andersson, S.G.1
  • 5
    • 0028803960 scopus 로고
    • Distinct roles for two purified factors in transcription of Xenopus mitochondrial DNA
    • Antoshechkin, I., and Bogenhagen, D.F. (1995). Distinct roles for two purified factors in transcription of Xenopus mitochondrial DNA. Mol. Cell. Biol. 15, 7032-7042.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 7032-7042
    • Antoshechkin, I.1    Bogenhagen, D.F.2
  • 6
    • 0026547544 scopus 로고
    • Nucleoid condensation in Escherichia coli that express a chlamydial histone homolog
    • Barry, C.E., III, Hayes, S.F., and Hackstadt, T. (1992). Nucleoid condensation in Escherichia coli that express a chlamydial histone homolog. Science 256, 377-379.
    • (1992) Science , vol.256 , pp. 377-379
    • Barry III, C.E.1    Hayes, S.F.2    Hackstadt, T.3
  • 7
    • 0027220445 scopus 로고
    • Hcl-mediated effects on DNA structure: A potential regulator of chlamydial development
    • Barry, C.E., III, Brickman, T.J., and Hackstadt, T. (1993). Hcl-mediated effects on DNA structure: a potential regulator of chlamydial development. Mol. Microbiol. 9, 273-283.
    • (1993) Mol. Microbiol. , vol.9 , pp. 273-283
    • Barry III, C.E.1    Brickman, T.J.2    Hackstadt, T.3
  • 8
    • 0018307726 scopus 로고
    • Characterization of a histone-like protein extracted from yeast mitochondria
    • Caron, F., Jacq, C., and Rouviere-Yaniv, J. (1979). Characterization of a histone-like protein extracted from yeast mitochondria. Proc. Natl. Acad. Sci. USA 76, 4265-4269.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4265-4269
    • Caron, F.1    Jacq, C.2    Rouviere-Yaniv, J.3
  • 9
    • 0028949844 scopus 로고
    • Cloning of an intrinsic human TFIID subunit that interacts with multiple transcriptional activators
    • Chiang, C.M., and Roeder, R.G. (1995). Cloning of an intrinsic human TFIID subunit that interacts with multiple transcriptional activators. Science 267, 531-536.
    • (1995) Science , vol.267 , pp. 531-536
    • Chiang, C.M.1    Roeder, R.G.2
  • 10
    • 0023413620 scopus 로고
    • Histone-like proteins of bacteria
    • Drlica, K., and Rouviere-Yaniv, J. (1987). Histone-like proteins of bacteria. Microbiol. Rev. 51, 301-319.
    • (1987) Microbiol. Rev. , vol.51 , pp. 301-319
    • Drlica, K.1    Rouviere-Yaniv, J.2
  • 12
    • 0025912955 scopus 로고
    • A close relative of the nuclear, chromosomal high-mobility group protein HMG1 in yeast mitochondria
    • Diffley, J.F.X., and Stillman, B. (1991). A close relative of the nuclear, chromosomal high-mobility group protein HMG1 in yeast mitochondria. Proc. Natl. Acad. Sci. USA 88, 7864-7868.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7864-7868
    • Diffley, J.F.X.1    Stillman, B.2
  • 13
    • 0026673872 scopus 로고
    • DNA binding properties of an HMG1-related protein from yeast mitochondria
    • Diffley, J.F.X., and Stillman, B. (1992). DNA binding properties of an HMG1-related protein from yeast mitochondria. J. Biol. Chem. 267, 3368-3374.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3368-3374
    • Diffley, J.F.X.1    Stillman, B.2
  • 14
    • 0024417597 scopus 로고
    • Role of the DNA/membrane complex in prokaryotic DNA replication
    • Firshein, W. (1989). Role of the DNA/membrane complex in prokaryotic DNA replication. Annu. Rev. Microbiol. 43, 89-120.
    • (1989) Annu. Rev. Microbiol. , vol.43 , pp. 89-120
    • Firshein, W.1
  • 15
    • 0023658329 scopus 로고
    • Promoter selection in human mitochondria involves binding of a transcription factor to orientation-independent upstream regulatory elements
    • Fisher, R.P., Topper, J.N., and Clayton, D.A. (1987). Promoter selection in human mitochondria involves binding of a transcription factor to orientation-independent upstream regulatory elements. Cell 50, 247-258.
    • (1987) Cell , vol.50 , pp. 247-258
    • Fisher, R.P.1    Topper, J.N.2    Clayton, D.A.3
  • 16
    • 0023684801 scopus 로고
    • Purification and characterization of human mitochondrial transcription factor 1
    • Fisher, R.P., and Clayton, D.A. (1988). Purification and characterization of human mitochondrial transcription factor 1. Mol. Cell. Biol. 8, 3496-3509.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3496-3509
    • Fisher, R.P.1    Clayton, D.A.2
  • 17
    • 0026640728 scopus 로고
    • DNA wrapping and bending by a mitochondrial high mobility group-like transcriptional activator protein
    • Fisher, R.P., Lisowsky, T., Parisi, M.A., and Clayton, D.A. (1992). DNA wrapping and bending by a mitochondrial high mobility group-like transcriptional activator protein. J. Biol. Chem. 267, 3358-3367.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3358-3367
    • Fisher, R.P.1    Lisowsky, T.2    Parisi, M.A.3    Clayton, D.A.4
  • 19
    • 0025215391 scopus 로고
    • The cell type-specific octamer transcription factor OTF-2 has two domains required for the activation of transcription
    • Gerster, T., Balmaceda, C.-G., and Roeder, R.G. (1990). The cell type-specific octamer transcription factor OTF-2 has two domains required for the activation of transcription. EMBO J. 9, 1635-1643.
    • (1990) EMBO J. , vol.9 , pp. 1635-1643
    • Gerster, T.1    Balmaceda, C.-G.2    Roeder, R.G.3
  • 20
    • 0028089747 scopus 로고
    • In organello footprint analysis of human mitochondrial DNA: Human mitochondrial transcription factor A interactions at the origin of replication
    • Ghivizzani, S., Madsen, C., Nelen, M., Ammmini, C., and Hauswirth, W. (1994). In organello footprint analysis of human mitochondrial DNA: human mitochondrial transcription factor A interactions at the origin of replication. Mol. Cell. Biol. 14, 7717-7730.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7717-7730
    • Ghivizzani, S.1    Madsen, C.2    Nelen, M.3    Ammmini, C.4    Hauswirth, W.5
  • 21
    • 0025870123 scopus 로고
    • Chlamydia trachomatis developmentally regulated protein is homologous to eukaryotic histone H1
    • Hackstadt, T., Baehr, W., and Ying, Y. (1991). Chlamydia trachomatis developmentally regulated protein is homologous to eukaryotic histone H1. Proc. Natl. Acad. Sci. USA 88, 3937-3941.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3937-3941
    • Hackstadt, T.1    Baehr, W.2    Ying, Y.3
  • 22
    • 0031991771 scopus 로고    scopus 로고
    • Cell cycle-dependent duplication and bidirectional migration of SeqA-associated DNA-protein complexes in E. coli
    • Hiraga, S., Ichinose, C., Niki, H., and Yamazoe, M. (1998). Cell cycle-dependent duplication and bidirectional migration of SeqA-associated DNA-protein complexes in E. coli. Mol. Cell 1, 381-387.
    • (1998) Mol. Cell. , vol.1 , pp. 381-387
    • Hiraga, S.1    Ichinose, C.2    Niki, H.3    Yamazoe, M.4
  • 23
    • 0842295026 scopus 로고
    • Nucleotide sequence of Bacillus subtilis dnaB: A gene essential for DNA replication initiation and membrane attachment
    • Hoshino, T., McKenzie, T., Schmidt, S., Tanaka, T., and Sueoka, N. (1987). Nucleotide sequence of Bacillus subtilis dnaB: a gene essential for DNA replication initiation and membrane attachment. Proc. Natl. Acad. Sci. USA 84, 653-657.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 653-657
    • Hoshino, T.1    McKenzie, T.2    Schmidt, S.3    Tanaka, T.4    Sueoka, N.5
  • 24
    • 0032128345 scopus 로고    scopus 로고
    • The Crithidia fasciculata KAP1 gene encodes a highly basic protein associated with kinetoplast DNA
    • Hines, J.C., and Ray, D.S. (1998). The Crithidia fasciculata KAP1 gene encodes a highly basic protein associated with kinetoplast DNA. Mol. Biol. Parasitol. 94, 41-52.
    • (1998) Mol. Biol. Parasitol. , vol.94 , pp. 41-52
    • Hines, J.C.1    Ray, D.S.2
  • 25
    • 0022398548 scopus 로고
    • Isolation and characterization of a membrane-DNA complex in the mitochondria of Physarum polycephalum
    • Kawano, S., and Kuroiwa, T, (1985). Isolation and characterization of a membrane-DNA complex in the mitochondria of Physarum polycephalum. Exp. Cell Res. 161, 460-472.
    • (1985) Exp. Cell Res. , vol.161 , pp. 460-472
    • Kawano, S.1    Kuroiwa, T.2
  • 26
    • 0000127106 scopus 로고
    • Proline-rich activator CTF1 targets the TFIIB assembly step during transcriptional activation
    • Kim, T.K., and Roeder, R.G. (1994). Proline-rich activator CTF1 targets the TFIIB assembly step during transcriptional activation. Proc. Natl. Acad. Sci. USA 91, 4170-4174.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4170-4174
    • Kim, T.K.1    Roeder, R.G.2
  • 28
    • 0016118765 scopus 로고
    • Studies on mitochondrial structure and function in Physarum polycephalum. III. Electron microscopy of a large amount of DNA releases from a central body in mitochondria by trypsin digestion
    • Kuroiwa, T. (1974). Studies on mitochondrial structure and function in Physarum polycephalum. III. Electron microscopy of a large amount of DNA releases from a central body in mitochondria by trypsin digestion. J. Cell Biol. 63, 299-306.
    • (1974) J. Cell Biol. , vol.63 , pp. 299-306
    • Kuroiwa, T.1
  • 29
    • 0017361760 scopus 로고
    • Studies on mitochondrial structure and function in Physarum polycephalum. V. Behaviour of mitochondrial nucleoids throughout mitochondrial division cycle
    • Kuroiwa, T., Kawano, S., and Hizume, M. (1977). Studies on mitochondrial structure and function in Physarum polycephalum. V. Behaviour of mitochondrial nucleoids throughout mitochondrial division cycle. J. Cell Biol. 72, 687-694.
    • (1977) J. Cell Biol. , vol.72 , pp. 687-694
    • Kuroiwa, T.1    Kawano, S.2    Hizume, M.3
  • 30
    • 0018902256 scopus 로고
    • Inhibition of Physarum mitochondrial division by cytochalasin B
    • Kuroiwa, T., and Kuroiwa, H. (1980). Inhibition of Physarum mitochondrial division by cytochalasin B. Experientia 36, 193-194.
    • (1980) Experientia , vol.36 , pp. 193-194
    • Kuroiwa, T.1    Kuroiwa, H.2
  • 31
    • 0020335569 scopus 로고
    • Mitochondrial nuclei
    • Kuroiwa, T. (1982). Mitochondrial nuclei. Int. Rev. Cytol. 75, 1-59.
    • (1982) Int. Rev. Cytol. , vol.75 , pp. 1-59
    • Kuroiwa, T.1
  • 32
    • 0028044696 scopus 로고
    • Molecular and cellular mechanisms of mitochondrial nuclear division and mitochondriokinesis
    • Kuroiwa, T., Ohta, T., Kuroiwa, H., and Kawano, S. (1994). Molecular and cellular mechanisms of mitochondrial nuclear division and mitochondriokinesis. Microsc. Res. Tech. 27, 220-232.
    • (1994) Microsc. Res. Tech. , vol.27 , pp. 220-232
    • Kuroiwa, T.1    Ohta, T.2    Kuroiwa, H.3    Kawano, S.4
  • 33
    • 0027646025 scopus 로고
    • A signature for the HMG-1 box DNA-binding proteins
    • Landsman, D., and Bustin, M. (1993). A signature for the HMG-1 box DNA-binding proteins. Bioessays 15, 539-546.
    • (1993) Bioessays , vol.15 , pp. 539-546
    • Landsman, D.1    Bustin, M.2
  • 34
    • 0029957097 scopus 로고    scopus 로고
    • A single mouse gene encodes the mitochondrial transcription factor A and a testis specific nuclear HMG-box protein
    • Larsson, N.G., Garman, J.D., Oldfors, A., Barsh, G.S., and Clayton, D.A. (1996). A single mouse gene encodes the mitochondrial transcription factor A and a testis specific nuclear HMG-box protein. Nat. Genet. 13, 296-302.
    • (1996) Nat. Genet. , vol.13 , pp. 296-302
    • Larsson, N.G.1    Garman, J.D.2    Oldfors, A.3    Barsh, G.S.4    Clayton, D.A.5
  • 35
    • 0016590613 scopus 로고
    • The attachment of the bacterial chromosome to the cell membrane
    • Liebowitz, P.J., and Schaechter, M. (1975). The attachment of the bacterial chromosome to the cell membrane. Int. Rev. Cytol. 41, 1-28.
    • (1975) Int. Rev. Cytol. , vol.41 , pp. 1-28
    • Liebowitz, P.J.1    Schaechter, M.2
  • 36
    • 0027242020 scopus 로고
    • Functional complementarity between the HMG1-like yeast mitochondrial histone HM and the bacterial histone-like protein HU
    • Megraw, T.L., and Chae, C.B. (1993). Functional complementarity between the HMG1-like yeast mitochondrial histone HM and the bacterial histone-like protein HU. J. Biol. Chem. 268, 12758-12763.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12758-12763
    • Megraw, T.L.1    Chae, C.B.2
  • 37
    • 0024340524 scopus 로고
    • The proline-rich transcriptional activator of CTF/NF-1 is distinct from the replication and DNA binding domain
    • Mermod, N., O'Neill, E.A., Kelly, T.J., and Tjian, R. (1989). The proline-rich transcriptional activator of CTF/NF-1 is distinct from the replication and DNA binding domain. Cell 58, 741-753.
    • (1989) Cell , vol.58 , pp. 741-753
    • Mermod, N.1    O'Neill, E.A.2    Kelly, T.J.3    Tjian, R.4
  • 38
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Miller, J.H. (1972). Experiments in Molecular Genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, pp. 201-205.
    • (1972) Experiments in Molecular Genetics , pp. 201-205
    • Miller, J.H.1
  • 39
    • 0021285523 scopus 로고
    • Fluorescence microscopic studies of mitochondrial nucleoids during meiosis and sporulation in the yeast, Saccharomyces cerevisiae
    • Miyakawa, I., Aoi, H., Sando, N., and Kuroiwa, T. (1984). Fluorescence microscopic studies of mitochondrial nucleoids during meiosis and sporulation in the yeast, Saccharomyces cerevisiae. J. Cell Sci. 66, 21-38.
    • (1984) J. Cell Sci. , vol.66 , pp. 21-38
    • Miyakawa, I.1    Aoi, H.2    Sando, N.3    Kuroiwa, T.4
  • 40
    • 0023442326 scopus 로고
    • Isolation of morphologically intact mitochondrial nucleoids from the yeast, Saccharomyces cerevisiae
    • Miyakawa, I., Sando, N., Kawano, S., Nakamura, S., and Kuroiwa, T. (1987). Isolation of morphologically intact mitochondrial nucleoids from the yeast, Saccharomyces cerevisiae. J. Cell Sci. 88, 431-439.
    • (1987) J. Cell Sci. , vol.88 , pp. 431-439
    • Miyakawa, I.1    Sando, N.2    Kawano, S.3    Nakamura, S.4    Kuroiwa, T.5
  • 41
    • 0029383841 scopus 로고
    • Characterization of DNA-binding proteins involved in the assembly of mitochondrial nucleoids in the yeast Saccharomyces cerevisiae
    • Miyakawa, I., Fumoto, S., Kuroiwa, T., and Sando, N. (1995). Characterization of DNA-binding proteins involved in the assembly of mitochondrial nucleoids in the yeast Saccharomyces cerevisiae. Plant Cell Physiol. 36, 1179-1188.
    • (1995) Plant Cell Physiol. , vol.36 , pp. 1179-1188
    • Miyakawa, I.1    Fumoto, S.2    Kuroiwa, T.3    Sando, N.4
  • 43
    • 78651128209 scopus 로고
    • Intramitochondrial fibers with DNA characteristics. I. Fixation and electron staining reactions
    • Nass, M.M.K., and Nass, S. (1963a). Intramitochondrial fibers with DNA characteristics. I. Fixation and electron staining reactions. J. Cell Biol. 19, 593-611.
    • (1963) J. Cell Biol. , vol.19 , pp. 593-611
    • Nass, M.M.K.1    Nass, S.2
  • 44
    • 78651121728 scopus 로고
    • Intramitochondrial fibers with DNA characteristics. II. Enzymatic and other hydrolytic treatments
    • Nass, M.M.K., and Nass, S. (1963b). Intramitochondrial fibers with DNA characteristics. II. Enzymatic and other hydrolytic treatments. J. Cell Biol. 19, 613-629.
    • (1963) J. Cell Biol. , vol.19 , pp. 613-629
    • Nass, M.M.K.1    Nass, S.2
  • 45
    • 0344808846 scopus 로고
    • The general occurrence of mitochondrial DNA
    • Nass, M.M.K., Nass, S., and Afzelius, B.A. (1965). The general occurrence of mitochondrial DNA. Exp. Cell Res. 37, 516-539.
    • (1965) Exp. Cell Res. , vol.37 , pp. 516-539
    • Nass, M.M.K.1    Nass, S.2    Afzelius, B.A.3
  • 46
    • 0027741381 scopus 로고
    • Restriction of amoebo-flagellate (AF) transformation to interphase is related to M phase replication of the centrosome complex in the amoebae of the true slime mould, Physarum polycephalum: A three-dimensional approach
    • Ohta, T., Kawano, S., and Kuroiwa, T. (1993). Restriction of amoebo-flagellate (AF) transformation to interphase is related to M phase replication of the centrosome complex in the amoebae of the true slime mould, Physarum polycephalum: a three-dimensional approach. J. Struct. Biol. 111, 105-117.
    • (1993) J. Struct. Biol. , vol.111 , pp. 105-117
    • Ohta, T.1    Kawano, S.2    Kuroiwa, T.3
  • 47
    • 0025829045 scopus 로고
    • Similarity of human mitochondrial transcription factor 1 to high mobility group proteins
    • Parisi, M.A., and Clayton, D.A. (1991). Similarity of human mitochondrial transcription factor 1 to high mobility group proteins. Science 252, 965-969.
    • (1991) Science , vol.252 , pp. 965-969
    • Parisi, M.A.1    Clayton, D.A.2
  • 48
    • 0016541064 scopus 로고
    • The chondriome of selected trypanosomatids. A three-dimensional study based on serial thick sections and high voltage electron microscopy
    • Paulin, J.J. (1975). The chondriome of selected trypanosomatids. A three-dimensional study based on serial thick sections and high voltage electron microscopy. J. Cell Biol. 66, 404-413.
    • (1975) J. Cell Biol. , vol.66 , pp. 404-413
    • Paulin, J.J.1
  • 49
    • 0032884687 scopus 로고    scopus 로고
    • The 25 kDa protein recognizing the rat curved region upstream of the origin of the L-strand replication is the rat homologue of the human mitochondrial transcription factor A
    • Pierro, P., Capaccio, L., and Gadaleta, G. (1999). The 25 kDa protein recognizing the rat curved region upstream of the origin of the L-strand replication is the rat homologue of the human mitochondrial transcription factor A. FEBS Lett. 457, 307-310.
    • (1999) FEBS Lett. , vol.457 , pp. 307-310
    • Pierro, P.1    Capaccio, L.2    Gadaleta, G.3
  • 50
    • 0343794843 scopus 로고
    • Characterization of a novel low-molecular -weight DNA-binding protein from Escherichia coli
    • Rouviere-Yaniv, J., and Gros, F. (1975). Characterization of a novel low-molecular -weight DNA-binding protein from Escherichia coli. Proc. Natl. Acad. Sci. USA 72, 3428-3432.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 3428-3432
    • Rouviere-Yaniv, J.1    Gros, F.2
  • 51
    • 0018405881 scopus 로고
    • E. coli DNA binding protein HU forms nucleosome like structure with circular double-stranded DNA
    • Rouviere-Yaniv, J., Yaniv, M., and Germond, J.E. (1979). E. coli DNA binding protein HU forms nucleosome like structure with circular double-stranded DNA. Cell 17, 265-274.
    • (1979) Cell , vol.17 , pp. 265-274
    • Rouviere-Yaniv, J.1    Yaniv, M.2    Germond, J.E.3
  • 52
    • 0028191858 scopus 로고
    • Behavior of mitochondria and their nuclei during amoebae cell proliferation in Physarum polycephalum
    • Sasaki, N., Suzuki, T., Ohta, T., Kawano, S., and Kuroiwa, T. (1994). Behavior of mitochondria and their nuclei during amoebae cell proliferation in Physarum polycephalum. Protoplasma 182, 115-125.
    • (1994) Protoplasma , vol.182 , pp. 115-125
    • Sasaki, N.1    Suzuki, T.2    Ohta, T.3    Kawano, S.4    Kuroiwa, T.5
  • 53
    • 0031715809 scopus 로고    scopus 로고
    • DNA synthesis in isolated mitochondrial nucleoids from plasmodia of Physarum polycephalum
    • Sasaki, N., Sakai, A., Kawano, S., Kuroiwa, H., and Kuroiwa, T. (1998). DNA synthesis in isolated mitochondrial nucleoids from plasmodia of Physarum polycephalum. Protoplasma 203, 221-231.
    • (1998) Protoplasma , vol.203 , pp. 221-231
    • Sasaki, N.1    Sakai, A.2    Kawano, S.3    Kuroiwa, H.4    Kuroiwa, T.5
  • 54
    • 0026054963 scopus 로고
    • Organization of multiple nucleoids and DNA molecules in mitochondria of a human
    • Satoh, M., and Kuroiwa, T. (1991). Organization of multiple nucleoids and DNA molecules in mitochondria of a human. Exp. Cell Res. 196, 137-140.
    • (1991) Exp. Cell Res. , vol.196 , pp. 137-140
    • Satoh, M.1    Kuroiwa, T.2
  • 55
    • 0025153881 scopus 로고
    • More than just histone-like proteins
    • Schmid, M.B. (1990). More than just histone-like proteins. Cell 63, 451-453.
    • (1990) Cell , vol.63 , pp. 451-453
    • Schmid, M.B.1
  • 56
    • 0022560051 scopus 로고
    • Kinetoplast DNA in trypanosomid flagellates
    • Simpson, L. (1986). Kinetoplast DNA in trypanosomid flagellates. Int. Rev. Cytol. 99, 119-179.
    • (1986) Int. Rev. Cytol. , vol.99 , pp. 119-179
    • Simpson, L.1
  • 57
    • 0024334775 scopus 로고
    • Histone H5 in the control of DNA synthesis and cell proliferation
    • Sun, J.M., Wiaderkiewicz, R., and Ruiz-Carrillo, A. (1989). Histone H5 in the control of DNA synthesis and cell proliferation. Science 245, 68-71.
    • (1989) Science , vol.245 , pp. 68-71
    • Sun, J.M.1    Wiaderkiewicz, R.2    Ruiz-Carrillo, A.3
  • 58
    • 0020335269 scopus 로고
    • Structure of three-dimensionally rod-shaped mitochondrial nucleoids isolated from the slime mould Physarum polycephalum
    • Suzuki, T., Kawano, S., and Kuroiwa, T. (1982). Structure of three-dimensionally rod-shaped mitochondrial nucleoids isolated from the slime mould Physarum polycephalum. J. Cell Sci. 58, 241-261.
    • (1982) J. Cell Sci. , vol.58 , pp. 241-261
    • Suzuki, T.1    Kawano, S.2    Kuroiwa, T.3
  • 61
  • 62
    • 0028093616 scopus 로고
    • The Oct-2 glutamine-rich and proline-rich activation domains can synergize with each other or duplicates of themselves to activate transcription
    • Tanaka, M., Clouston, W.M., and Herr, W. (1994). The Oct-2 glutamine-rich and proline-rich activation domains can synergize with each other or duplicates of themselves to activate transcription. Mol. Cell. Biol. 14, 6046-6055.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6046-6055
    • Tanaka, M.1    Clouston, W.M.2    Herr, W.3
  • 63
    • 0018581187 scopus 로고
    • Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin
    • Thoma, F., Koller, T., and Klug, A. (1979). Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin. J. Cell Biol. 83, 403-427.
    • (1979) J. Cell Biol. , vol.83 , pp. 403-427
    • Thoma, F.1    Koller, T.2    Klug, A.3
  • 64
    • 0030052478 scopus 로고    scopus 로고
    • Nucleus-encoded histone H1-like proteins are associated with kinetoplast DNA in the Trypanosomatid Crithidia fasciculata
    • Xu, C.W., Hines, J.C., Engel, M.L., Russell, D.G., and Ray, D.S. (1996). Nucleus-encoded histone H1-like proteins are associated with kinetoplast DNA in the Trypanosomatid Crithidia fasciculata. Mol. Cell. Biol. 16, 564-576.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 564-576
    • Xu, C.W.1    Hines, J.C.2    Engel, M.L.3    Russell, D.G.4    Ray, D.S.5
  • 65
    • 0028097921 scopus 로고
    • The structure and function of proline-rich regions in proteins
    • Williamson, M.P. (1994). The structure and function of proline-rich regions in proteins. Biochem. J. 297, 249-260.
    • (1994) Biochem. J. , vol.297 , pp. 249-260
    • Williamson, M.P.1
  • 66
    • 0024267577 scopus 로고
    • Construction and characterization of the deletion mutant of hupA and hupB genes in Escherichia coli
    • Wada, M., Kano, Y., Ogawa, T., Okazaki, T., and Imamoto, F. (1988). Construction and characterization of the deletion mutant of hupA and hupB genes in Escherichia coli. J. Mol. Biol. 204, 581-591.
    • (1988) J. Mol. Biol. , vol.204 , pp. 581-591
    • Wada, M.1    Kano, Y.2    Ogawa, T.3    Okazaki, T.4    Imamoto, F.5
  • 68
    • 0344020676 scopus 로고
    • Membrane attachment activates dnaA protein, the initiation protein of chromosome replication in Escherichia coli
    • Yung, B.Y., and Kornberg, A. (1988). Membrane attachment activates dnaA protein, the initiation protein of chromosome replication in Escherichia coli. Proc. Natl. Acad. Sci. USA 85, 7202-7205.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7202-7205
    • Yung, B.Y.1    Kornberg, A.2
  • 69
    • 0031943922 scopus 로고    scopus 로고
    • Functions of high mobility group protein, Abf2p, in mitochondrial DNA segregation, recombination and copy number in Saccharomyces cerevisiae
    • Zelenaya-Troitskaya, O., Newman, S.M., Okamoto, K., Perlman, P.S., and Butow, R.A. (1998). Functions of high mobility group protein, Abf2p, in mitochondrial DNA segregation, recombination and copy number in Saccharomyces cerevisiae. Genetics 148, 1763-1776.
    • (1998) Genetics , vol.148 , pp. 1763-1776
    • Zelenaya-Troitskaya, O.1    Newman, S.M.2    Okamoto, K.3    Perlman, P.S.4    Butow, R.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.