Improvement in pHERD vectors to express recombinant proteins tagged with hexahistidine at either the NH2- or COOH- terminal in Pseudomonas aeruginosa

研究成果: ジャーナルへの寄稿記事

抄録

We constructed pHERDHis vectors to express polyhistidine-tagged proteins based on the pHERD vectors. The oligonucleotides containing the hexahistidine sequence were designed to be able to introduce the tag at either the NH2- or COOH- terminal. To demonstrate the usefulness of the vectors, a pyocyanin biosynthetic protein, PhzS, was expressed in a pyocyanin-deficient mutant of Pseudomonas aeruginosa. In the mutant strain, both HisPhzS (tag at the NH2- terminal) and PhzSHis (tag at the COOH- terminal) worked as a functional protein and pyocyanin was produced. It was also demonstrated that HisPhzS was purified by standard affinity chromatography.

元の言語英語
ページ(範囲)57-61
ページ数5
ジャーナルJournal of Insect Biotechnology and Sericology
80
発行部数2
出版物ステータス出版済み - 6 1 2012

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His-His-His-His-His-His
Pyocyanine
Recombinant proteins
Recombinant Proteins
Pseudomonas aeruginosa
recombinant proteins
Proteins
Affinity chromatography
mutants
proteins
Oligonucleotides
affinity chromatography
oligonucleotides
Affinity Chromatography
pyocyanin
Recombinant
Tag
Protein

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Applied Microbiology and Biotechnology
  • Business, Management and Accounting(all)
  • Agricultural and Biological Sciences(all)
  • Insect Science
  • Industrial and Manufacturing Engineering

これを引用

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title = "Improvement in pHERD vectors to express recombinant proteins tagged with hexahistidine at either the NH2- or COOH- terminal in Pseudomonas aeruginosa",
abstract = "We constructed pHERDHis vectors to express polyhistidine-tagged proteins based on the pHERD vectors. The oligonucleotides containing the hexahistidine sequence were designed to be able to introduce the tag at either the NH2- or COOH- terminal. To demonstrate the usefulness of the vectors, a pyocyanin biosynthetic protein, PhzS, was expressed in a pyocyanin-deficient mutant of Pseudomonas aeruginosa. In the mutant strain, both HisPhzS (tag at the NH2- terminal) and PhzSHis (tag at the COOH- terminal) worked as a functional protein and pyocyanin was produced. It was also demonstrated that HisPhzS was purified by standard affinity chromatography.",
author = "Kazuhiro Iiyama and Lee, {Jae Man} and Takahiro Kusakabe and Chisa Yasunaga-Aoki and Susumu Shimizu",
year = "2012",
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language = "English",
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journal = "Journal of Insect Biotechnology and Sericology",
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T1 - Improvement in pHERD vectors to express recombinant proteins tagged with hexahistidine at either the NH2- or COOH- terminal in Pseudomonas aeruginosa

AU - Iiyama, Kazuhiro

AU - Lee, Jae Man

AU - Kusakabe, Takahiro

AU - Yasunaga-Aoki, Chisa

AU - Shimizu, Susumu

PY - 2012/6/1

Y1 - 2012/6/1

N2 - We constructed pHERDHis vectors to express polyhistidine-tagged proteins based on the pHERD vectors. The oligonucleotides containing the hexahistidine sequence were designed to be able to introduce the tag at either the NH2- or COOH- terminal. To demonstrate the usefulness of the vectors, a pyocyanin biosynthetic protein, PhzS, was expressed in a pyocyanin-deficient mutant of Pseudomonas aeruginosa. In the mutant strain, both HisPhzS (tag at the NH2- terminal) and PhzSHis (tag at the COOH- terminal) worked as a functional protein and pyocyanin was produced. It was also demonstrated that HisPhzS was purified by standard affinity chromatography.

AB - We constructed pHERDHis vectors to express polyhistidine-tagged proteins based on the pHERD vectors. The oligonucleotides containing the hexahistidine sequence were designed to be able to introduce the tag at either the NH2- or COOH- terminal. To demonstrate the usefulness of the vectors, a pyocyanin biosynthetic protein, PhzS, was expressed in a pyocyanin-deficient mutant of Pseudomonas aeruginosa. In the mutant strain, both HisPhzS (tag at the NH2- terminal) and PhzSHis (tag at the COOH- terminal) worked as a functional protein and pyocyanin was produced. It was also demonstrated that HisPhzS was purified by standard affinity chromatography.

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