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

• Published in: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology Vol. 140; no. 2; pp. 207 - 210
• Main Authors: Nakamura, Morihiko, Tanigawa, Y.
• Format: Journal Article
• Language: English
• Published: England Elsevier Inc 01.02.2005
• Subjects: Animals; Apoptosis; Chromatin; GST; Histone 2A; Histones - metabolism; Kinetics; Lymphokine; Mice; Protein Binding; Recombinant Fusion Proteins - chemistry; Recombinant Fusion Proteins - metabolism; Suppressor factor; Suppressor Factors, Immunologic - chemistry; Suppressor Factors, Immunologic - genetics; Suppressor Factors, Immunologic - metabolism; T cell; Ubiquitin-like protein; Ubiquitins - chemistry; Histone 2A; Chromatin; T cell; GST; Lymphokine; Ubiquitin-like protein; Suppressor factor; Apoptosis
• ISSN: 1096-4959; 1879-1107
• DOI: 10.1016/j.cbpc.2004.09.030

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.