Purification of bacteriophage λO protein that specifically binds to the origin of replication

Toshiki Tsurimoto, Kenichi Matsubara

研究成果: ジャーナルへの寄稿記事

20 引用 (Scopus)

抄録

By means of a nitrocellulose filter binding assay, DNA binding activities among proteins fractionated from extracts of Escherichia coli carrying λdv have been surveyed. An activity was found that binds specifically to a fragment of 164 base pairs that specifies the λ replication origin (λ ori). This activity was not detected in an extract of cells not carrying the λdv plasmid. The activity was detected in extracts of cells carrying a hybrid plasmid in which the entire λ O gene had been cloned and placed under the control of the lac promoter. Deletion of a 60 base pair segment in the 'amino-terminal region' of the O gene abolished this activity, indicating that the λ ori binding protein is coded for by the λ O gene. The ori-specific binding protein was purified by five fractionation steps. The most purified preparation consists of a major polypeptide that migrates with a molecular weight of 32,000 in SDS-polyacrylamide gel electrophoresis. Binding of O protein to ori occurs in the absence of other protein aceous components.

元の言語英語
ページ(範囲)325-331
ページ数7
ジャーナルMGG Molecular & General Genetics
181
発行部数3
DOI
出版物ステータス出版済み - 3 1 1981
外部発表Yes

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Replication Origin
Bacteriophages
Carrier Proteins
Cell Extracts
Base Pairing
Plasmids
Genes
Proteins
Collodion
Polyacrylamide Gel Electrophoresis
Molecular Weight
Escherichia coli
Peptides
DNA

All Science Journal Classification (ASJC) codes

  • Genetics

これを引用

Purification of bacteriophage λO protein that specifically binds to the origin of replication. / Tsurimoto, Toshiki; Matsubara, Kenichi.

:: MGG Molecular & General Genetics, 巻 181, 番号 3, 01.03.1981, p. 325-331.

研究成果: ジャーナルへの寄稿記事

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