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In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
11:36

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Published on: July 25, 2019

Noncovalent interaction of MNSFbeta, a ubiquitin-like protein, with histone 2A

Morihiko Nakamura1, Y Tanigawa

  • 1Cooperative Medical Research Center, Shimane University, 89-1 Enya-cho, Izumo 693-8501, Japan. nkmr0515@med.shimane-u.ac.jp

Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology
|January 15, 2005
PubMed

Monoclonal nonspecific suppressor factor (MNSF), a lymphokine produced by murine T cell hybridoma, possesses pleiotrophic antigen-nonspecific suppressive functions. A cDNA clone encoding MNSFbeta, an isoform of the MNSF, has been isolated and characterized. MNSFbeta 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.

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