کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10840390 | 1067677 | 2005 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Co-immunoprecipitation of Hsp101 with cytosolic Hsc70
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Co-immunoprecipitation of Hsp101 with cytosolic Hsc70 Co-immunoprecipitation of Hsp101 with cytosolic Hsc70](/preview/png/10840390.png)
چکیده انگلیسی
In animals and yeast, cytosolic Hsp70s function in concert with other molecular chaperones. Hsp70 is a major chaperone in the Hsp90 multi-chaperone complexes that participate in maturation of steroid receptors and several other proteins. Hsp70s also appear to form a complex with Hsp90 and Hsp110/sHsp. A 100 kDa protein was co-immunoprecipitated with cytosolic Hsc70 from maize seedlings (Zea mays). The presence of this complex was further confirmed using gel-filtration chromatography. Mass spectrometric analysis showed that the 100 kDa protein is homologous with Arabidopsis Hsp101. Treatment with apyrase enhanced the co-immunoprecipitation of Hsp101 with Hsc70, while ATP had the opposite effect. In the presence of carboxymethylated α-lactalbumin (CMLA), which is permanently unfolded, the complex dissociated. Based on these observations, it is concluded that Hsc70 and Hsp101 are present in a complex in the plant cytosol.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Plant Physiology and Biochemistry - Volume 43, Issue 1, January 2005, Pages 13-18
Journal: Plant Physiology and Biochemistry - Volume 43, Issue 1, January 2005, Pages 13-18
نویسندگان
Chun Zhang, Charles L. Guy,