ID | 74539 |
Title Transcription | チュウトウド コウネツセイ サイキン Geobacillus stearothermophilus セイイク オンド ヘンイカブ ニ オケル タンパクシツ ハツゲン カイセキ
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Title Alternative | Protein Expression Analysis in Temparature-adaptated Mutant Strains of Moderately thermophile Geobacillus stearothermophilus
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Author |
Kyogoku, Hitomi
Laboratory of Biochemistry, Department of Mathematical and Natural Sciences, Faculty of Integrated Arts and Sciences, The University of Tokushima
Yamaguchi, Yasuaki
Laboratory of Biochemistry, Department of Mathematical and Natural Sciences, Faculty of Integrated Arts and Sciences, The University of Tokushima
Miyano-Ono, Momoyo
Laboratory of Biochemistry, Department of Mathematical and Natural Sciences, Faculty of Integrated Arts and Sciences, The University of Tokushima
Yamaguchi, Ayano
Laboratory of Biochemistry, Department of Mathematical and Natural Sciences, Faculty of Integrated Arts and Sciences, The University of Tokushima
Satoh, Takanori
Laboratory of Biochemistry, Department of Mathematical and Natural Sciences, Faculty of Integrated Arts and Sciences, The University of Tokushima
KAKEN Search Researchers
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Keywords | Thermophile
Adaptation
Expression
Growth temperature
Geobacillus stearothermophilus
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Content Type |
Departmental Bulletin Paper
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Description | Optimum growth of moderately thermophile Geobacillus stearothermophilus (Bst) has been observed at 55ºC, and suppressed by the downshift to lower temperature. In order to understand the relationship between growth temperature and protein expression, we made Bst mutant strains which were adapted to lower temperature (30ºC) compared with wild type strain, and then we examined their protein expression under various growth temperatures. When they were cultured at 55ºC, different expression patterns of six proteins (P1-P6) were observed between wild type and mutant strains, whereas five proteins (A1-A5) were found only in mutant strains cultured at 37ºC. Furthermore, expression of five proteins (DS1-DS5) was increased according to the downshift of growth temperature to 37ºC. Among all 16 proteins, abundant three proteins (P1, DS3, and DS5) were electroblotted to PVDF membrane, followed by analyzed N-terminal amino acid sequences. As a result, it was suggested that P1 must be Surface-layer protein A (sbsA), whereas DS3 and DS5 were unknown proteins.
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Journal Title |
徳島大学総合科学部自然科学研究 = Natural Science Research, The University of Tokushima
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ISSN | 09146385
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NCID | AN10065859
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Volume | 23
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Issue | 3
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Start Page | 87
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End Page | 95
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Sort Key | 87
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Published Date | 2009-10
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EDB ID | |
FullText File | |
language |
jpn
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TextVersion |
Publisher
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departments |
Science and Technology
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