書誌事項
- タイトル別名
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- Characterization of a Novel Mammalian Co-chaperone, DnaJB7, an HSP40 Family Member
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抄録
Molecular chaperones of HSP70 family members usually work together with HSP40/DNAJ family members in protein biogenesis and protein homeostasis. In mammals, approximately 50 members of the HSP40/DNAJ family are identified so far. Here, we isolated a cDNA clone of DnaJB7, one of the HSP40/DNAJ family members, and examined the properties of DnaJB7 protein in vivo and in vitro . Since the DnaJB7 gene in the human genome has no obvious heat shock element (HSE), DnaJB7 could not be induced by heat shock in HeLa cells. While overexpressed DnaJB7 in HeLa cells was distributed to both the cytoplasm and nucleolus at normal temperature, upon heat shock it accumulated in the nucleolus, where it co-localized with Hsp70. This localization pattern was very similar to that of Hsp40 (DnaJB1). Direct interaction of Hsp70 with DnaJB7 in HeLa cells was demonstrated by immunoprecipitation. Also, DnaJB7 could stimulate the ATPase activity of Hsp70. Hsp70 had molecular chaperone activity in suppressing aggregation of heat denatured luciferase, and DnaJB7 could facilitate the chaperone activity of Hsp70. In murine tissues, DnaJB7 was highly expressed in the stomach and faintly in pancreas, uterus and ovary. These results suggest that DnaJB7 is a stomach-enriched co-chaperone of Hsp70.
収録刊行物
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- Thermal Medicine
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Thermal Medicine 27 (1), 9-23, 2010
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詳細情報 詳細情報について
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- CRID
- 1390001205285931264
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- NII論文ID
- 10028165528
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- NII書誌ID
- AN10084762
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- ISSN
- 18823750
- 18822576
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- NDL書誌ID
- 11062582
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
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- 抄録ライセンスフラグ
- 使用不可