메뉴 건너뛰기




Volumn 145, Issue 1, 1996, Pages 41-48

Overproduction, purification and characterization of the HPB12-L24 ribosomal protein of Bacillus subtilis

Author keywords

Bacillus subtilis; Gel retardation; Histone like protein; L24 ribosomal protein; Nucleoid; Overproduction; Purification

Indexed keywords

AMMONIUM SULFATE; DNA; HISTONE; RIBOSOME PROTEIN;

EID: 0030589074     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/0378-1097(96)00383-7     Document Type: Article
Times cited : (4)

References (19)
  • 1
    • 0022000472 scopus 로고
    • Isolation and characterization of small heat-stable DNA-binding proteins from Bacillus subtilis nucleoid
    • [1] Salti, V., Le Hégarat, F. and Hirschbein, L. (1985) Isolation and characterization of small heat-stable DNA-binding proteins from Bacillus subtilis nucleoid. J. Gen. Microbiol. 131, 581-590.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 581-590
    • Salti, V.1    Le Hégarat, F.2    Hirschbein, L.3
  • 2
    • 0027411091 scopus 로고
    • Purification and characterization of the HLJ-like protein HPB9 from the Bacillus subtilis nucleoid
    • [2] Le Hégarat, F., Salti-Montesanto, V., Hauck, Y. and Hirschbein, L. (1993) Purification and characterization of the HLJ-like protein HPB9 from the Bacillus subtilis nucleoid. Biochim. Biophys. Acta 1172, 101-107.
    • (1993) Biochim. Biophys. Acta , vol.1172 , pp. 101-107
    • Le Hégarat, F.1    Salti-Montesanto, V.2    Hauck, Y.3    Hirschbein, L.4
  • 3
    • 0024461907 scopus 로고
    • Purification and properties of the DNA-binding protein HPB12 from the Bacillus subtilis Nucleoid
    • [3] Salti, V., Le Hégarat, F., Fontaine, Y. and Hirschbein, L. (1989) Purification and properties of the DNA-binding protein HPB12 from the Bacillus subtilis Nucleoid. Biochim. Biophys. Acta 1009, 161-167.
    • (1989) Biochim. Biophys. Acta , vol.1009 , pp. 161-167
    • Salti, V.1    Le Hégarat, F.2    Fontaine, Y.3    Hirschbein, L.4
  • 6
    • 0024449327 scopus 로고
    • Cloning and analysis of the spc ribosomal protein operon of Bacillus subtilis: Comparison with the spc operon of E. Coli
    • [6] Henkin, T.M., Moon, S.H., Mattheakis, L.C. and Nomura, M. (1989) Cloning and analysis of the spc ribosomal protein operon of Bacillus subtilis: Comparison with the spc operon of E. coli. Nucleic Acids Res. 17, 7469-7486.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 7469-7486
    • Henkin, T.M.1    Moon, S.H.2    Mattheakis, L.C.3    Nomura, M.4
  • 7
    • 0022372670 scopus 로고
    • Enzymatic amplification of β-globin genomic sequences and restriction site analysis for diagnostic of sickle cell anemia
    • [7] Saïki, R.K., Scharf, S., Floona, F., Mullis, K., Horn, G., Erlich, H.A. and Arnheim, N. (1985) Enzymatic amplification of β-globin genomic sequences and restriction site analysis for diagnostic of sickle cell anemia. Science 230, 1350-1354.
    • (1985) Science , vol.230 , pp. 1350-1354
    • Saïki, R.K.1    Scharf, S.2    Floona, F.3    Mullis, K.4    Horn, G.5    Erlich, H.A.6    Arnheim, N.7
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • [8] Bradford, M.N. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.N.1
  • 9
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of the head of bacteriophage T4
    • [9] Laemmli, U.K. (1970) Cleavage of structural protein during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 10
    • 0026642903 scopus 로고
    • Three microtubules organizing centers are required for ascus growth and sporulation in the fungus Sordaria macrospora
    • [10] Thompson-Coffe, C. and Zickler, D. (1992) Three microtubules organizing centers are required for ascus growth and sporulation in the fungus Sordaria macrospora. Cell Motil. Cytoskeleton 22, 257-273.
    • (1992) Cell Motil. Cytoskeleton , vol.22 , pp. 257-273
    • Thompson-Coffe, C.1    Zickler, D.2
  • 11
    • 0023948010 scopus 로고
    • High efficiency transformation of E. Coli by high voltage electroporation
    • [11] Dower, W.J., Miller, J.F. and Ragsdale, C.W. (1988) High efficiency transformation of E. coli by high voltage electroporation. Nucleic Acids Res. 16, 6127-6145.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 6127-6145
    • Dower, W.J.1    Miller, J.F.2    Ragsdale, C.W.3
  • 12
    • 0025153881 scopus 로고
    • More than just 'histone-like' proteins
    • [12] 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
  • 13
    • 0026451648 scopus 로고
    • HU, the major histone-like protein of E. Coli, modulates the binding of IHF to oric
    • [13] Bonnefoy, E. and Rouviere-Yaniv, J. (1992) HU, the major histone-like protein of E. coli, modulates the binding of IHF to oriC. EMBO J. 11, 4489-4496.
    • (1992) EMBO J. , vol.11 , pp. 4489-4496
    • Bonnefoy, E.1    Rouviere-Yaniv, J.2
  • 14
    • 0023424964 scopus 로고
    • Spontaneous missense mutations in the rplx gene for the ribosomal protein L24 from Escherichia coli
    • [14] Nishi, K., Müller, M. and Schnier, J. (1987) Spontaneous Missense Mutations in the rplx gene for the ribosomal protein L24 from Escherichia coli. J. Bacteriol. 169, 4854-4856.
    • (1987) J. Bacteriol. , vol.169 , pp. 4854-4856
    • Nishi, K.1    Müller, M.2    Schnier, J.3
  • 15
    • 4244214917 scopus 로고
    • (Gualerzi, C.O. and Pon, C.L. Eds.), Springer-Verlag, Berlin
    • [15] Le Hégarat, F., Salti, V. and Hirschbein, L. (1986) In: Bacterial Chromatin (Gualerzi, C.O. and Pon, C.L. Eds.), pp. 155-166, Springer-Verlag, Berlin.
    • (1986) Bacterial Chromatin , pp. 155-166
    • Le Hégarat, F.1    Salti, V.2    Hirschbein, L.3
  • 17
    • 0029974453 scopus 로고    scopus 로고
    • Extraribosomal functions of ribosomal proteins
    • [17] Wool, I. (1996) Extraribosomal functions of ribosomal proteins. Trends Biochem. Sci. 21, 164-165.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 164-165
    • Wool, I.1
  • 18
    • 0024206339 scopus 로고
    • Translational regulation of the spc operon in Escherichia coli. Identification and structural analysis of the target sit for S8 represser protein
    • [18] Cerriti, D.P., Mattheakis, L., Kearney, K.R., Vu, L. and Nomura, M. (1988) Translational regulation of the spc operon in Escherichia coli. Identification and structural analysis of the target sit for S8 represser protein. J. Mol. Biol. 204, 309-325.
    • (1988) J. Mol. Biol. , vol.204 , pp. 309-325
    • Cerriti, D.P.1    Mattheakis, L.2    Kearney, K.R.3    Vu, L.4    Nomura, M.5
  • 19
    • 0026573628 scopus 로고
    • Lethal overproduction of the Escherichia coli nucleoid protein H-NS: Ultramicroscopic and molecular autopsy
    • [19] Spurio, R., Dürrenberger, M., Falconi, M., Teana, A.L., Pon, C.L. and Gualerzi., C. (1992) Lethal overproduction of the Escherichia coli nucleoid protein H-NS: ultramicroscopic and molecular autopsy. Mol. Gen. Genet. 231, 201-211.
    • (1992) Mol. Gen. Genet. , vol.231 , pp. 201-211
    • Spurio, R.1    Dürrenberger, M.2    Falconi, M.3    Teana, A.L.4    Pon, C.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.