کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10820691 | 1060730 | 2005 | 4 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Noncovalent interaction of MNSFbeta, a ubiquitin-like protein, with histone 2A
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Noncovalent interaction of MNSFbeta, a ubiquitin-like protein, with histone 2A Noncovalent interaction of MNSFbeta, a ubiquitin-like protein, with histone 2A](/preview/png/10820691.png)
چکیده انگلیسی
Monoclonal nonspecific suppressor factor (MNSF), a lymphokine produced by murine T cell hybridoma, possesses pleiotrophic antigen-nonspecific suppressive functions. A cDNA clone encoding MNSFβ, an isoform of the MNSF, has been isolated and characterized. MNSFβ cDNA encodes a fusion protein consisting of a ubiquitin-like segment (Ubi-L) and ribosomal protein S30. Most recently, we observed that Ubi-L covalently conjugates to Bcl-G, a novel pro-apoptotic protein. In this study, we observed that Ubi-L noncovalently and specifically binds to histone 2A. The maximum binding was observed at a molar ratio equal to 1 for GST-Ubi-L and 2 for histone 2A. Ubi-L formed complex with histone 2A in the presence of 1% Triton X-100. Free Ubi-L was detected in nuclei from unstimulated murine helper T cell line, D10. The increased amounts of free Ubi-L and some Ubi-L adducts were observed in nuclei from mitogen-activated D10 cells. Interestingly, two Ubi-L adducts were unique to the chromatin fraction of nuclei from the activated D10 cells.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology - Volume 140, Issue 2, February 2005, Pages 207-210
Journal: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology - Volume 140, Issue 2, February 2005, Pages 207-210
نویسندگان
Morihiko Nakamura, Y. Tanigawa,