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Purification and Characterization of a DNA-Binding Protein of Vibrio cholerae O1

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Title: Purification and Characterization of a DNA-Binding Protein of Vibrio cholerae O1
Authors: Ehara, Masahiko / Ichinose, Yoshio / Iwami, Mamoru / Utsunomiya, Akiyoshi / Shimotori, Shoichi
Issue Date: 30-Sep-1991
Publisher: 長崎大学熱帯医学研究所 / Institute of Tropical Medicine, Nagasaki University
Citation: 熱帯医学 Tropical medicine 33(3). p67-82, 1991
Abstract: A DNA-Binding protein was purified from the cell-surface of Vibrio cholerae O1 by Cellulofine Sulfate affinity chromatography and reversed-phase HPLC. The DNA-binding protein of V. cholerae O1 showed a molecular weight of 9 kDa estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Treatment of the protein with cold acetone and 6 M guanidine-HCl produced little change in the DNA-binding activity of the protein. The binding of the protein to supercoiled plasmid DNA as well as to double-stranded short chromosomal DNA fragments has been demonstrated by gel retardation assay and by labeling of the transblotted protein with non-radioactive DNA. N-terminal amino acid sequence of the protein showed a high degree of homology with that of HU 2 (Laine et al., 1978), NS2 (Mende et al., 1978) from Escherichia coli. Indirect immunocytochemical labeling of ultrathin sections of Lowicryl-embedded V. cholerae O1 cells with the antibody against the protein revealed that the protein associates with bulk DNA and also lies at the cell-surface.
URI: http://hdl.handle.net/10069/4584
ISSN: 03855643
Type: Departmental Bulletin Paper
Appears in Collections:Volume 33, No. 3

Citable URI : http://hdl.handle.net/10069/4584

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