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著作: [友安 俊文]/[田端 厚之]/[長宗 秀明]/Investigation of the chaperone function of the small heat shock protein AgsA./[BMC Biochemistry]

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EID
214680
EOID
661726
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0
LastModified
2012年9月24日(月) 12:28:05
Operator
大家 隆弘
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友安 俊文
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種別 必須 学術論文(審査論文)
言語 必須 英語
招待 推奨 依頼
審査 推奨 Peer Review
カテゴリ 推奨 研究
共著種別 推奨
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著者 必須
  1. 友安 俊文([徳島大学.大学院社会産業理工学研究部.生物資源産業学域.応用生命系.生体分子機能学分野]/[徳島大学.生物資源産業学部.生物資源産業学科.応用生命講座])
    役割 任意
    貢献度 任意
    学籍番号 推奨
  2. 田端 厚之([徳島大学.大学院社会産業理工学研究部.生物資源産業学域.応用生命系.生体分子機能学分野]/[徳島大学.生物資源産業学部.生物資源産業学科.応用生命講座])
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    学籍番号 推奨
  3. 長宗 秀明
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題名 必須

(英) Investigation of the chaperone function of the small heat shock protein AgsA.

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(英) A small heat shock protein AgsA was originally isolated from Salmonella enterica serovar Typhimurium. We previously demonstrated that AgsA was an effective chaperone that could reduce the amount of heat-aggregated proteins in an Escherichia coli rpoH mutant. AgsA appeared to promote survival at lethal temperatures by cooperating with other chaperones in vivo. To investigate the aggregation prevention mechanisms of AgsA, we constructed N- or C-terminal truncated mutants and compared their properties with wild type AgsA. AgsA showed significant overall homology to wheat sHsp16.9 allowing its three-dimensional structure to be predicted. Truncations of AgsA until the N-terminal 23rd and C-terminal 11th amino acid (AA) from both termini preserved its in vivo chaperone activity. Temperature-controlled gel filtration chromatography showed that purified AgsA could maintain large oligomeric complexes up to 50 degrees C. Destabilization of oligomeric complexes was observed for N-terminal 11- and 17-AA truncated AgsA; C-terminal 11-AA truncated AgsA could not form large oligomeric complexes. AgsA prevented the aggregation of denatured lysozyme, malate dehydrogenase (MDH) and citrate synthase (CS) but did not prevent the aggregation of insulin at 25 degrees C. N-terminal 17-AA truncated AgsA showed no chaperone activity towards MDH. C-terminal 11-AA truncated AgsA showed weak or no chaperone activity towards lysozyme, MDH and CS although it prevented the aggregation of insulin at 25 degrees C. When the same amount of AgsA and C-terminal 11-AA truncated AgsA were mixed (half of respective amount required for efficient chaperone activities), good chaperone activity for all substrates and temperatures was observed. Detectable intermolecular exchanges between AgsA oligomers at 25 degrees C were not observed using fluorescence resonance energy transfer analysis; however, significant exchanges between AgsA oligomers and C-terminal truncated AgsA were observed at 25 degrees C. Our data demonstrate that AgsA has several regions necessary for efficient chaperone activity: region(s) important for lysozyme chaperone activity are located outer surface of the oligomeric complex while those region(s) important for insulin are located inside the oligomeric complex and those for MDH are located within the N-terminal arm. In addition, the equilibrium between the oligomer and the dimer structures appears to be important for its efficient chaperone activity.

キーワード 推奨
  1. (英) chaperone / (日) シャペロン
発行所 推奨 BioMed Central Ltd.
誌名 必須 BMC Biochemistry([BioMed Central Ltd.])
(eISSN: 1471-2091)
ISSN 任意 1471-2091
ISSN: 1471-2091 (eISSN: 1471-2091)
Title: BMC biochemistry
Title(ISO): BMC Biochem
Publisher: BioMed Central
 (NLM Catalog  (Scopus  (CrossRef (Scopus information is found. [need login])
必須 11
必須 ---
必須 27 27
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年月日 必須 2010年 6月 24日
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DOI 任意 10.1186/1471-2091-11-27    (→Scopusで検索)
PMID 任意 20653971    (→Scopusで検索)
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  1. (英) Article.Affiliation: Department of Biological Science and Technology, Institute of Technology and Science, The University of Tokushima Graduate School, Minami-josanjima-cho, Tokushima 770-8506, Japan. tomoyasu@bio.tokushima-u.ac.jp

  2. (英) Article.PublicationTypeList.PublicationType: Journal Article

  3. (英) Article.PublicationTypeList.PublicationType: Research Support, Non-U.S. Gov't

  4. (英) OtherID: PMC2920228