PMID: 9540822Apr 16, 1998Paper

Conjugation of ubiquitin-like polypeptide to intracellular acceptor proteins

Biochimica Et Biophysica Acta
T NagataY Tanigawa

Abstract

Monoclonal nonspecific suppressor factor (MNSF), a lymphokine produced by a murine hybridoma, was originally found to inhibit the generation of LPS-induced immunoglobulin secreting cells. MNSF comprises of MNSF beta, an isoform of MNSF, and the other isoform, MNSF alpha. Ubiquitin-like segment (Ubi-L) of MNSF beta shows MNSF-like activity. Ubi-L (7.8 kDa) has 36% homology with 8.5 kDa ubiquitin. GST-Ubi-L was labeled with 125I by the chloramine T method and tested for its conjugation to acceptor in splenocyte lysates. 125I-GST-Ubi-L conjugation on SDS-PAGE showed heterogeneous bands including 95 kDa GST-Ubi-L conjugation in the splenocyte, but not reticulocyte lysates. The Ubi-L adduct appeared to be MNSF-related molecule because anti-MNSF monoclonal antibody (mAb) recognized the 95 kDa band. The pattern of the conjugations was different from that seen in ubiquitination. Unlabeled GST-Ubi-L inhibited the conjugations, while ubiquitin did not. alpha-Lactalbumin, one of the target proteins for ubiquitination, failed to conjugate to GST-Ubi-L. In addition, covalent conjugation of ubiquitin to reticulocyte lysates was also interfered by GST-Ubi-L. These results suggest that Ubi-L may conjugate to acceptor proteins in a similar, but...Continue Reading

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Citations

Aug 3, 2005·Nature Reviews. Molecular Cell Biology·Rebecca L WelchmanR John Mayer
May 15, 2002·Biochimica Et Biophysica Acta·Morihiko NakamuraYoshinori Tanigawa
Jun 11, 1999·The Journal of Biological Chemistry·M Nakamura, Y Tanigawa

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