메뉴 건너뛰기




Volumn 182, Issue 7, 2000, Pages 1942-1948

The Bacillus subtilis Hbsu protein modifies the effects of α/β-type, small acid-soluble spore proteins on DNA

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; BACTERIAL PROTEIN;

EID: 0034022882     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.7.1942-1948.2000     Document Type: Article
Times cited : (25)

References (49)
  • 1
    • 0030928287 scopus 로고    scopus 로고
    • Repressor induced site-specific binding of HU for transcriptional regulation
    • Aki, T., and S. Adhya. 1997. Repressor induced site-specific binding of HU for transcriptional regulation. EMBO J. 16:3666-3674.
    • (1997) EMBO J. , vol.16 , pp. 3666-3674
    • Aki, T.1    Adhya, S.2
  • 2
    • 0032496659 scopus 로고    scopus 로고
    • Characterization of yhcN, a new forespore-specific gene of Bacillus subtilis
    • Bagyan, I., M. Noback, S. Bron, M. Paidhungat, and P. Setlow. 1998. Characterization of yhcN, a new forespore-specific gene of Bacillus subtilis. Gene 212:179-188.
    • (1998) Gene , vol.212 , pp. 179-188
    • Bagyan, I.1    Noback, M.2    Bron, S.3    Paidhungat, M.4    Setlow, P.5
  • 3
    • 0032444114 scopus 로고    scopus 로고
    • New small, acid-soluble proteins unique to spores of Bacillus subtilis: Identification of the coding genes and regulation and function of two of these genes
    • Bagyan, I., B. Setlow, and P. Setlow. 1998. New small, acid-soluble proteins unique to spores of Bacillus subtilis: identification of the coding genes and regulation and function of two of these genes. J. Bacteriol. 180:6704-6712.
    • (1998) J. Bacteriol. , vol.180 , pp. 6704-6712
    • Bagyan, I.1    Setlow, B.2    Setlow, P.3
  • 4
    • 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., and J. Rouviere-Yaniv. 1991. HU and IHF, two homologous histone-like proteins of Escherichia coli, form different protein-DNA complexes with short DNA fragments. EMBO J. 10:687-696.
    • (1991) EMBO J. , vol.10 , pp. 687-696
    • Bonnefoy, E.1    Rouviere-Yaniv, J.2
  • 5
    • 0029039656 scopus 로고
    • Theory of the mobility-shift assay of nonspecific protein-DNA complexes governed by conditional probabilities: The HU:DNA complex
    • Cann, J. R., O. Pfenninger, and D. E. Pettijohn. 1995. Theory of the mobility-shift assay of nonspecific protein-DNA complexes governed by conditional probabilities: the HU:DNA complex. Electrophoresis 16:881-887.
    • (1995) Electrophoresis , vol.16 , pp. 881-887
    • Cann, J.R.1    Pfenninger, O.2    Pettijohn, D.E.3
  • 6
    • 0021992147 scopus 로고
    • Cloning of a small, acid-soluble spore protein gene from Bacillus subtilis and determination of its complete nucleotide sequence
    • Connors, M. J., and P. Setlow. 1985. Cloning of a small, acid-soluble spore protein gene from Bacillus subtilis and determination of its complete nucleotide sequence. J. Bacteriol. 161:333-339.
    • (1985) J. Bacteriol. , vol.161 , pp. 333-339
    • Connors, M.J.1    Setlow, P.2
  • 7
    • 0021346918 scopus 로고
    • Protein HU in the enzymatic replication of the chromosomal origin of Escherichia coli
    • Dixon, N. E., and A. Kornberg. 1984. Protein HU in the enzymatic replication of the chromosomal origin of Escherichia coli. Proc. Natl. Acad. Sci. USA 81:424-428.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 424-428
    • Dixon, N.E.1    Kornberg, A.2
  • 8
    • 0025853061 scopus 로고
    • Inhibition of cell division in hupA hupB mutant bacteria lacking HU protein
    • Dri, A.-M., J. Rouvier-Yaniv, and P. L. Moreau. 1991. Inhibition of cell division in hupA hupB mutant bacteria lacking HU protein. J. Bacteriol. 173:2852-2863.
    • (1991) J. Bacteriol. , vol.173 , pp. 2852-2863
    • Dri, A.-M.1    Rouvier-Yaniv, J.2    Moreau, P.L.3
  • 9
    • 0024198720 scopus 로고
    • Immunoelectron microscopic localization of small, acid-soluble spore proteins in sporulating cells of Bacillus subtilis
    • Francesconi, S. C., T. J. MacAlister, B. Setlow, and P. Setlow. 1988. Immunoelectron microscopic localization of small, acid-soluble spore proteins in sporulating cells of Bacillus subtilis. J. Bacteriol. 170:5963-5967.
    • (1988) J. Bacteriol. , vol.170 , pp. 5963-5967
    • Francesconi, S.C.1    MacAlister, T.J.2    Setlow, B.3    Setlow, P.4
  • 10
    • 0027990219 scopus 로고
    • Electron microscopic studies of the interaction between a Bacillus subtilis α/β-type small, acid-soluble spore protein with DNA: Protein binding is cooperative, stiffens the DNA, and induces negative supercoiling
    • Griffith, J., A. Makhov, L. Santiago-Lara, and P. Setlow. 1994. Electron microscopic studies of the interaction between a Bacillus subtilis α/β-type small, acid-soluble spore protein with DNA: protein binding is cooperative, stiffens the DNA, and induces negative supercoiling. Proc. Natl. Acad. Sci. USA 91:8224-8228.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8224-8228
    • Griffith, J.1    Makhov, A.2    Santiago-Lara, L.3    Setlow, P.4
  • 11
    • 0026651448 scopus 로고
    • Determination of DNA-binding parameters for the Bacillus subtilis histone-like HBsu protein through introduction of fluorophores by site-directed mutagenesis of a synthetic gene
    • Groch, N., H. Schindelin, A. S. Scholtz, U. Hahn, and U. Heinemann. 1992 Determination of DNA-binding parameters for the Bacillus subtilis histone-like HBsu protein through introduction of fluorophores by site-directed mutagenesis of a synthetic gene. Eur. J. Biochem. 207:677-685.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 677-685
    • Groch, N.1    Schindelin, H.2    Scholtz, A.S.3    Hahn, U.4    Heinemann, U.5
  • 12
    • 0029017527 scopus 로고
    • Use of immunofluorescence to visualize cell-specific gene expression during sporulation in Bacillus subtilis
    • Harry, E. J., K. Pogliano, and R. Losick. 1995. Use of immunofluorescence to visualize cell-specific gene expression during sporulation in Bacillus subtilis. J. Bacteriol. 177:3386-3393.
    • (1995) J. Bacteriol. , vol.177 , pp. 3386-3393
    • Harry, E.J.1    Pogliano, K.2    Losick, R.3
  • 13
    • 0030884116 scopus 로고    scopus 로고
    • Analysis of deamidation of small, acid-soluble spore proteins from Bacillus subtilis in vitro and in vivo
    • Hayes, C. S., and P. Setlow. 1997. Analysis of deamidation of small, acid-soluble spore proteins from Bacillus subtilis in vitro and in vivo. J. Bacteriol. 179:6020-6027.
    • (1997) J. Bacteriol. , vol.179 , pp. 6020-6027
    • Hayes, C.S.1    Setlow, P.2
  • 16
    • 0030904358 scopus 로고    scopus 로고
    • Association of the histone-like protein HBsu with the nucleoid of Bacillus subtilis
    • Kohler, P., and M. A. Marahiel. 1997. Association of the histone-like protein HBsu with the nucleoid of Bacillus subtilis. J. Bacteriol. 179:2060-2064.
    • (1997) J. Bacteriol. , vol.179 , pp. 2060-2064
    • Kohler, P.1    Marahiel, M.A.2
  • 17
    • 0030731108 scopus 로고    scopus 로고
    • The complete genome sequence of the gram-positive bacterium Bacillus subtilis
    • Kunst, F., N. Ogasawara, I. Moszer, A. M. Albertini, G. Alloni, et al. 1997. The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature 390:249-256.
    • (1997) Nature , vol.390 , pp. 249-256
    • Kunst, F.1    Ogasawara, N.2    Moszer, I.3    Albertini, A.M.4    Alloni, G.5
  • 18
    • 0029973105 scopus 로고    scopus 로고
    • Anatomy of a flexer-DNA complex inside a higher-order transposition intermediate
    • Lavoie, B., G. S. Shaw, A. Millner, and G. Chaconas. 1996. Anatomy of a flexer-DNA complex inside a higher-order transposition intermediate. Cell 85:761-771.
    • (1996) Cell , vol.85 , pp. 761-771
    • Lavoie, B.1    Shaw, G.S.2    Millner, A.3    Chaconas, G.4
  • 19
    • 0031858092 scopus 로고    scopus 로고
    • Escherichia coli strains lacking protein HU are UV sensitive due to a role for HU in homologous recombination
    • Li, S., and R. Waters. 1998. Escherichia coli strains lacking protein HU are UV sensitive due to a role for HU in homologous recombination. J. Bacteriol. 180:3750-3756.
    • (1998) J. Bacteriol. , vol.180 , pp. 3750-3756
    • Li, S.1    Waters, R.2
  • 20
    • 0023051656 scopus 로고
    • Proteins from the prokaryotic nucleoid. A protein-protein cross-linking study on the quaternary structure of Escherichia coli DNA-binding protein NS (HU)
    • Losso, M. A., R. T. Pawlik, M. A. Canonaco, and C. O. Gualerzi. 1986. Proteins from the prokaryotic nucleoid. A protein-protein cross-linking study on the quaternary structure of Escherichia coli DNA-binding protein NS (HU). Eur. J. Biochem. 155:27-32.
    • (1986) Eur. J. Biochem. , vol.155 , pp. 27-32
    • Losso, M.A.1    Pawlik, R.T.2    Canonaco, M.A.3    Gualerzi, C.O.4
  • 22
    • 0029974595 scopus 로고    scopus 로고
    • Analysis of the relationship between the decrease in pH and accumulation of 3-phosphoglyceric acid in developing forespores of Bacillus species
    • Magill, N. G., A. E. Cowan, M. A. Leyva-Vazquez, M. Brown, D. E. Koppel, et al. 1996. Analysis of the relationship between the decrease in pH and accumulation of 3-phosphoglyceric acid in developing forespores of Bacillus species. J. Bacteriol. 178:2204-2210.
    • (1996) J. Bacteriol. , vol.178 , pp. 2204-2210
    • Magill, N.G.1    Cowan, A.E.2    Leyva-Vazquez, M.A.3    Brown, M.4    Koppel, D.E.5
  • 23
    • 0025897381 scopus 로고
    • Molecular cloning, nucleotide sequence, and characterization of the Bacillus subtilis gene encoding the DNA-binding protein HBsu
    • Micka, B., N. Groch, U. Heinemann, and M. A. Marahiel. 1991. Molecular cloning, nucleotide sequence, and characterization of the Bacillus subtilis gene encoding the DNA-binding protein HBsu. J. Bacteriol. 173:3191-3198.
    • (1991) J. Bacteriol. , vol.173 , pp. 3191-3198
    • Micka, B.1    Groch, N.2    Heinemann, U.3    Marahiel, M.A.4
  • 24
    • 0026702673 scopus 로고
    • The DNA-binding protein HBsu is essential for normal growth and development in Bacillus subtilis
    • Micka, B., and M. A. Marahiel. 1992. The DNA-binding protein HBsu is essential for normal growth and development in Bacillus subtilis. Biochimie 74:641-650.
    • (1992) Biochimie , vol.74 , pp. 641-650
    • Micka, B.1    Marahiel, M.A.2
  • 25
    • 0025640779 scopus 로고
    • Binding of DNA in vitro by a small, acid-soluble spore protein from Bacillus subtilis and the effect of this binding on DNA topology
    • Nicholson, W. L., B. Setlow, and P. Setlow. 1990. Binding of DNA in vitro by a small, acid-soluble spore protein from Bacillus subtilis and the effect of this binding on DNA topology. J. Bacteriol. 172:6900-6906.
    • (1990) J. Bacteriol. , vol.172 , pp. 6900-6906
    • Nicholson, W.L.1    Setlow, B.2    Setlow, P.3
  • 26
    • 0026002937 scopus 로고
    • Ultraviolet irradiation of DNA complexed with α/β-type small, acid-soluble proteins from spores of Bacillus or Clostridium species makes spore photoproduct but not thymine dimers
    • Nicholson, W. L., B. Setlow, and P. Setlow. 1991. Ultraviolet irradiation of DNA complexed with α/β-type small, acid-soluble proteins from spores of Bacillus or Clostridium species makes spore photoproduct but not thymine dimers. Proc. Natl. Acad. Sci. USA 88:8288-8292.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8288-8292
    • Nicholson, W.L.1    Setlow, B.2    Setlow, P.3
  • 27
    • 0025057959 scopus 로고
    • Dramatic increase in negative superhelicity of plasmid DNA in the forespore compartment of sporulating cells of Bacillus subtilis
    • Nicholson, W. L., and P. Setlow. 1990. Dramatic increase in negative superhelicity of plasmid DNA in the forespore compartment of sporulating cells of Bacillus subtilis. J. Bacteriol. 172:7-14.
    • (1990) J. Bacteriol. , vol.172 , pp. 7-14
    • Nicholson, W.L.1    Setlow, P.2
  • 28
    • 0001864545 scopus 로고
    • Sporulation, germination and outgrowth
    • C. R. Harwood and S. M. Cutting (ed.), Wiley, New York, N.Y.
    • Nicholson, W. L., and P. Setlow. 1990. Sporulation, germination and outgrowth, p. 391-450. In C. R. Harwood and S. M. Cutting (ed.), Molecular biology methods for Bacillus. Wiley, New York, N.Y.
    • (1990) Molecular Biology Methods for Bacillus , pp. 391-450
    • Nicholson, W.L.1    Setlow, P.2
  • 29
    • 0026648406 scopus 로고
    • The DNA-binding protein HU from mesophilic and thermophilic bacilli: Gene cloning, overproduction and purification
    • Padas, P. M., K. S. Wilson, and C. E. Vorgias. 1992. The DNA-binding protein HU from mesophilic and thermophilic bacilli: gene cloning, overproduction and purification. Gene 117:39-44.
    • (1992) Gene , vol.117 , pp. 39-44
    • Padas, P.M.1    Wilson, K.S.2    Vorgias, C.E.3
  • 30
    • 0033515646 scopus 로고    scopus 로고
    • Differential binding of the Escherichia coli HU, homodimeric forms and heterodimeric form to linear, gapped and cruciform DNA
    • Pinson, V., M. Takahashi, and J. Rouviere-Yaniv. 1999. Differential binding of the Escherichia coli HU, homodimeric forms and heterodimeric form to linear, gapped and cruciform DNA. J. Mol. Biol. 287:485-497.
    • (1999) J. Mol. Biol. , vol.287 , pp. 485-497
    • Pinson, V.1    Takahashi, M.2    Rouviere-Yaniv, J.3
  • 31
    • 0029610802 scopus 로고
    • Visualization of the suhcellular location of sporulation proteins in Bacillus subtilis using immunofluorescence microscopy
    • Pogliano, K., E. Harry, and R. Losick. 1995. Visualization of the suhcellular location of sporulation proteins in Bacillus subtilis using immunofluorescence microscopy. Mol. Microbiol. 18:459-470.
    • (1995) Mol. Microbiol. , vol.18 , pp. 459-470
    • Pogliano, K.1    Harry, E.2    Losick, R.3
  • 32
    • 0017629285 scopus 로고
    • Localization of the HU protein on the Escherichia coli nucleoid
    • Ronviere-Yaniv, J. 1978. Localization of the HU protein on the Escherichia coli nucleoid. Cold Spring Harbor Symp. Quant. Biol. 42:439-447.
    • (1978) Cold Spring Harbor Symp. Quant. Biol. , vol.42 , pp. 439-447
    • Ronviere-Yaniv, J.1
  • 33
    • 0343794843 scopus 로고
    • Characterization of a novel, low-molecular-weight DNA-binding protein from Escherichia coli
    • Rouviere-Yaniv, J., and F. Gros. 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
  • 34
    • 0018644060 scopus 로고
    • Native Escherichia coli HU protein is a heterotypic dimer
    • Rouviere-Yaniv, J., and N. O. Kjeldgaard. 1979. Native Escherichia coli HU protein is a heterotypic dimer. FEBS Lett. 104:297-300.
    • (1979) FEBS Lett. , vol.104 , pp. 297-300
    • Rouviere-Yaniv, J.1    Kjeldgaard, N.O.2
  • 35
    • 0018405881 scopus 로고
    • E. coli DNA binding protein HU forms nucleosome-like structure with circular double-stranded DNA
    • Rouviere-Yaniv, J., and M. Yaniv. 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
  • 37
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H., and G. Von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 38
    • 70349368703 scopus 로고
    • Determination of nucleic acids in tissues by pentose analysis
    • Schneider, W. C. 1957. Determination of nucleic acids in tissues by pentose analysis. Methods Enzymol. 3:680-684.
    • (1957) Methods Enzymol. , vol.3 , pp. 680-684
    • Schneider, W.C.1
  • 39
    • 0023118953 scopus 로고
    • Thymine-containing dimers as well as spore photoproducts are found in ultraviolet-irradiated Bacillus subtilis spores that lack small acid-soluble proteins
    • Setlow, B., and P. Setlow. 1987. Thymine-containing dimers as well as spore photoproducts are found in ultraviolet-irradiated Bacillus subtilis spores that lack small acid-soluble proteins. Proc. Natl. Acad. Sci. USA 84:421-423.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 421-423
    • Setlow, B.1    Setlow, P.2
  • 40
    • 0026547858 scopus 로고
    • Interaction between DNA and α/β-type small, acid-soluble spore proteins: A new class of DNA-binding protein
    • Setlow, B., D. Sun, and P. Setlow. 1992. Interaction between DNA and α/β-type small, acid-soluble spore proteins: a new class of DNA-binding protein. J. Bacteriol. 174:2312-2322.
    • (1992) J. Bacteriol. , vol.174 , pp. 2312-2322
    • Setlow, B.1    Sun, D.2    Setlow, P.3
  • 41
    • 0003158423 scopus 로고
    • Changes in the forespore chromosome structure during sporulation in Bacillus species
    • Setlow, P. 1991. Changes in the forespore chromosome structure during sporulation in Bacillus species. Semin. Dev. Biol. 2:55-62.
    • (1991) Semin. Dev. Biol. , vol.2 , pp. 55-62
    • Setlow, P.1
  • 42
    • 0028868465 scopus 로고
    • Mechanisms for the prevention of damage to DNA in spores of Bacillus species
    • Setlow, P. 1995. Mechanisms for the prevention of damage to DNA in spores of Bacillus species. Annu. Rev. Microbiol. 49:29-54.
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 29-54
    • Setlow, P.1
  • 44
    • 0021286693 scopus 로고
    • 3-A resolution structure of a protein with histone-like properties in prokaryotes
    • Tanaka, I., K. Appelt, J. Dijk, S. W. White, and K. S. Wilson. 1984. 3-A resolution structure of a protein with histone-like properties in prokaryotes. Nature 310:376-381.
    • (1984) Nature , vol.310 , pp. 376-381
    • Tanaka, I.1    Appelt, K.2    Dijk, J.3    White, S.W.4    Wilson, K.S.5
  • 45
    • 0025914934 scopus 로고
    • Effects of mutant small, acid-soluble spore proteins from Bacillus subtilis on DNA in vivo and in vitro
    • Tovar-Rojo, F., and P. Setlow. 1991. Effects of mutant small, acid-soluble spore proteins from Bacillus subtilis on DNA in vivo and in vitro. J. Bacteriol. 173:4827-4835.
    • (1991) J. Bacteriol. , vol.173 , pp. 4827-4835
    • Tovar-Rojo, F.1    Setlow, P.2
  • 46
    • 0023029113 scopus 로고
    • Use of a lacZ gene fusion to determine the dependence pattern of sporulation operon spoIIIC in spo mutants of Bacillus subtilis: A branched pathway of expression of sporulation operons
    • Turner, S. M., J. Mandelstam, and J. Errington. 1986. Use of a lacZ gene fusion to determine the dependence pattern of sporulation operon spoIIIC in spo mutants of Bacillus subtilis: a branched pathway of expression of sporulation operons. J. Gen. Microbiol. 132:2995-3003.
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 2995-3003
    • Turner, S.M.1    Mandelstam, J.2    Errington, J.3
  • 47
    • 0024267577 scopus 로고
    • Construction and characterization of the deletion mutant of hupA and hupB genes in Escherichia coli
    • Wada, M., T. Ogawa, T. Okazaki, and F. Imamoto. 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    Ogawa, T.2    Okazaki, T.3    Imamoto, F.4
  • 49
    • 0030926466 scopus 로고    scopus 로고
    • HU protein binding to the replication origin of the rolling-circle plasmid pKYM enhances DNA replication
    • Yasukawa, H., E. Ozaki, K. Nakahama, and Y. Masamune. 1997. HU protein binding to the replication origin of the rolling-circle plasmid pKYM enhances DNA replication. Mol. Gen. Genet. 254:548-554.
    • (1997) Mol. Gen. Genet. , vol.254 , pp. 548-554
    • Yasukawa, H.1    Ozaki, E.2    Nakahama, K.3    Masamune, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.