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Heat shock protein 60 negatively regulates the biological functions of ubiquitin-like protein MNSFβ in macrophages

Authors
  • Nakamura, Morihiko1
  • Notsu, Kaori1
  • Nakagawa, Mai1
  • 1 Shimane University, Division of Regional Collaborative Medical Research, Office for Regional Collaboration and Innovation, Izumo, 693-8501, Japan , Izumo (Japan)
Type
Published Article
Journal
Molecular and Cellular Biochemistry
Publisher
Springer-Verlag
Publication Date
Feb 01, 2019
Volume
456
Issue
1-2
Pages
29–39
Identifiers
DOI: 10.1007/s11010-018-3487-5
Source
Springer Nature
Keywords
License
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Abstract

Monoclonal nonspecific suppressor factor β (MNSFβ) is a ubiquitously expressed ubiquitin-like protein known to be involved in various biological functions. Previous studies have demonstrated that MNSFβ covalently modify its target proteins including Bcl-G, a proapoptotic protein. In this study, we purified a 65 kDa MNSFβ adduct from mouse liver lysates by sequential chromatography on DEAE and glutathione S-transferase (GST)-fusioned MNSFβ immobilized on glutathione-Sepharose beads in the presence of ATP. MALDI-TOF mass spectrometry fingerprinting revealed that this MNSFβ adduct consists of an 8.5 kDa MNSFβ and heat shock protein 60 (HSP60), a mitochondrial protein involved in protein folding. Fingerprinting analysis of the MNSFβ adduct demonstrates that MNSFβ conjugates to HSP60 with a linkage between the C-terminal Gly74 and Lys481. HSP60 siRNA neutralized the inhibition of apoptosis by MNSFβ siRNA in LPS/IFNγ-stimulated Raw264.7, a murine macrophage cell line. HSP60 siRNA also down-regulated the enhancement of TNFα production by MNSFβ siRNA in LPS-stimulated Raw264.7 cells. Here, we firstly report that MNSFβ activity is negatively regulated by molecular chaperone.

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