Stimulation of expression of a silica-induced protein (Sip) in Thermus thermophilus by supersaturated silicic acid

Katsumi Doi, Yasuhiro Fujino, Fumio Inagaki, Ryouichi Kawatsu, Miki Tahara, Toshihisa Ohshima, Yoshihiro Okaue, Takushi Yokoyama, Satoru Iwai, Seiya Ogata

研究成果: ジャーナルへの寄稿記事

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抄録

The effects of silicic acid on the growth of Thermus thermophilus TMY, an extreme thermophile isolated from a siliceous deposit formed from geothermal water at a geothermal power plant in Japan, were examined at 75°C. At concentrations higher than the solubility of amorphous silica (400 to 700 ppm SiO2), a silica-induced protein (Sip) was isolated from the cell envelope fraction of log-phase TMY cells grown in the presence of supersaturated silicic acid. Two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed the molecular mass and pI of Sip to be about 35 kDa and 9.5, respectively. Induction of Sip expression occurred within 1 h after the addition of a supersaturating concentration of silicic acid to TM broth. Expression of Sip-like proteins was also observed in other thermophiles, including T. thermophilus HB8 and Thermus aquaticus YT-1. The amino acid sequence of Sip was similar to that of the predicted solute-binding protein of the Fe3+ ABC transporter in T. thermophilus HB8 (locus tag, TTHA1628; GenBank accession no. NC-006461; GeneID, 3169376). The sip gene (987-bp) product showed 87% identity with the TTHA1628 product and the presumed Fe 3+-binding protein of T. thermophilus HB27 (locus tag TTC1264; GenBank accession no. NC-005835; GeneID, 2774619). Within the genome, sip is situated as a component of the Fbp-type ABC transporter operon, which contains a palindromic structure immediately downstream of sip. This structure is conserved in other T. thermophilus genomes and may function as a terminator that causes definitive Sip expression in response to silica stress.

元の言語英語
ページ(範囲)2406-2413
ページ数8
ジャーナルApplied and environmental microbiology
75
発行部数8
DOI
出版物ステータス出版済み - 4 1 2009

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Thermus thermophilus
Silicic Acid
silicic acid
Silicon Dioxide
silica
protein
Proteins
thermophilic microorganisms
proteins
ABC transporters
ATP-Binding Cassette Transporters
Nucleic Acid Databases
binding proteins
Carrier Proteins
Thermus aquaticus
protein synthesis
Thermus
Genome
genome
siliceous deposit

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Food Science
  • Applied Microbiology and Biotechnology
  • Ecology

これを引用

Stimulation of expression of a silica-induced protein (Sip) in Thermus thermophilus by supersaturated silicic acid. / Doi, Katsumi; Fujino, Yasuhiro; Inagaki, Fumio; Kawatsu, Ryouichi; Tahara, Miki; Ohshima, Toshihisa; Okaue, Yoshihiro; Yokoyama, Takushi; Iwai, Satoru; Ogata, Seiya.

:: Applied and environmental microbiology, 巻 75, 番号 8, 01.04.2009, p. 2406-2413.

研究成果: ジャーナルへの寄稿記事

Doi, Katsumi ; Fujino, Yasuhiro ; Inagaki, Fumio ; Kawatsu, Ryouichi ; Tahara, Miki ; Ohshima, Toshihisa ; Okaue, Yoshihiro ; Yokoyama, Takushi ; Iwai, Satoru ; Ogata, Seiya. / Stimulation of expression of a silica-induced protein (Sip) in Thermus thermophilus by supersaturated silicic acid. :: Applied and environmental microbiology. 2009 ; 巻 75, 番号 8. pp. 2406-2413.
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abstract = "The effects of silicic acid on the growth of Thermus thermophilus TMY, an extreme thermophile isolated from a siliceous deposit formed from geothermal water at a geothermal power plant in Japan, were examined at 75°C. At concentrations higher than the solubility of amorphous silica (400 to 700 ppm SiO2), a silica-induced protein (Sip) was isolated from the cell envelope fraction of log-phase TMY cells grown in the presence of supersaturated silicic acid. Two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed the molecular mass and pI of Sip to be about 35 kDa and 9.5, respectively. Induction of Sip expression occurred within 1 h after the addition of a supersaturating concentration of silicic acid to TM broth. Expression of Sip-like proteins was also observed in other thermophiles, including T. thermophilus HB8 and Thermus aquaticus YT-1. The amino acid sequence of Sip was similar to that of the predicted solute-binding protein of the Fe3+ ABC transporter in T. thermophilus HB8 (locus tag, TTHA1628; GenBank accession no. NC-006461; GeneID, 3169376). The sip gene (987-bp) product showed 87{\%} identity with the TTHA1628 product and the presumed Fe 3+-binding protein of T. thermophilus HB27 (locus tag TTC1264; GenBank accession no. NC-005835; GeneID, 2774619). Within the genome, sip is situated as a component of the Fbp-type ABC transporter operon, which contains a palindromic structure immediately downstream of sip. This structure is conserved in other T. thermophilus genomes and may function as a terminator that causes definitive Sip expression in response to silica stress.",
author = "Katsumi Doi and Yasuhiro Fujino and Fumio Inagaki and Ryouichi Kawatsu and Miki Tahara and Toshihisa Ohshima and Yoshihiro Okaue and Takushi Yokoyama and Satoru Iwai and Seiya Ogata",
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T1 - Stimulation of expression of a silica-induced protein (Sip) in Thermus thermophilus by supersaturated silicic acid

AU - Doi, Katsumi

AU - Fujino, Yasuhiro

AU - Inagaki, Fumio

AU - Kawatsu, Ryouichi

AU - Tahara, Miki

AU - Ohshima, Toshihisa

AU - Okaue, Yoshihiro

AU - Yokoyama, Takushi

AU - Iwai, Satoru

AU - Ogata, Seiya

PY - 2009/4/1

Y1 - 2009/4/1

N2 - The effects of silicic acid on the growth of Thermus thermophilus TMY, an extreme thermophile isolated from a siliceous deposit formed from geothermal water at a geothermal power plant in Japan, were examined at 75°C. At concentrations higher than the solubility of amorphous silica (400 to 700 ppm SiO2), a silica-induced protein (Sip) was isolated from the cell envelope fraction of log-phase TMY cells grown in the presence of supersaturated silicic acid. Two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed the molecular mass and pI of Sip to be about 35 kDa and 9.5, respectively. Induction of Sip expression occurred within 1 h after the addition of a supersaturating concentration of silicic acid to TM broth. Expression of Sip-like proteins was also observed in other thermophiles, including T. thermophilus HB8 and Thermus aquaticus YT-1. The amino acid sequence of Sip was similar to that of the predicted solute-binding protein of the Fe3+ ABC transporter in T. thermophilus HB8 (locus tag, TTHA1628; GenBank accession no. NC-006461; GeneID, 3169376). The sip gene (987-bp) product showed 87% identity with the TTHA1628 product and the presumed Fe 3+-binding protein of T. thermophilus HB27 (locus tag TTC1264; GenBank accession no. NC-005835; GeneID, 2774619). Within the genome, sip is situated as a component of the Fbp-type ABC transporter operon, which contains a palindromic structure immediately downstream of sip. This structure is conserved in other T. thermophilus genomes and may function as a terminator that causes definitive Sip expression in response to silica stress.

AB - The effects of silicic acid on the growth of Thermus thermophilus TMY, an extreme thermophile isolated from a siliceous deposit formed from geothermal water at a geothermal power plant in Japan, were examined at 75°C. At concentrations higher than the solubility of amorphous silica (400 to 700 ppm SiO2), a silica-induced protein (Sip) was isolated from the cell envelope fraction of log-phase TMY cells grown in the presence of supersaturated silicic acid. Two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed the molecular mass and pI of Sip to be about 35 kDa and 9.5, respectively. Induction of Sip expression occurred within 1 h after the addition of a supersaturating concentration of silicic acid to TM broth. Expression of Sip-like proteins was also observed in other thermophiles, including T. thermophilus HB8 and Thermus aquaticus YT-1. The amino acid sequence of Sip was similar to that of the predicted solute-binding protein of the Fe3+ ABC transporter in T. thermophilus HB8 (locus tag, TTHA1628; GenBank accession no. NC-006461; GeneID, 3169376). The sip gene (987-bp) product showed 87% identity with the TTHA1628 product and the presumed Fe 3+-binding protein of T. thermophilus HB27 (locus tag TTC1264; GenBank accession no. NC-005835; GeneID, 2774619). Within the genome, sip is situated as a component of the Fbp-type ABC transporter operon, which contains a palindromic structure immediately downstream of sip. This structure is conserved in other T. thermophilus genomes and may function as a terminator that causes definitive Sip expression in response to silica stress.

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