期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 286, 期 16, 页码 14291-14303出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110.204602
关键词
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资金
- Czech Science Foundation [P304/10/0868]
- Ministry of Defense, Czech Republic [FVZ0000604]
- Ministry of Education, Youth, and Sports of the Czech Republic [LC07017]
- Institutional Research Concept [AV0Z50200510]
- Regional Center for Applied Molecular Oncology [CZ.1.05/2.1.00/03.0101]
- Cancer Research UK [C377/A6355]
The interferon-regulated transcription factor and tumor suppressor protein IRF-1 is predicted to be largely disordered outside of the DNA-binding domain. One of the advantages of intrinsically disordered protein domains is thought to be their ability to take part in multiple, specific but low affinity protein interactions; however, relatively few IRF-1-interacting proteins have been described. The recent identification of a functional binding interface for the E3-ubiquitin ligase CHIP within the major disordered domain of IRF-1 led us to ask whether this region might be employed more widely by regulators of IRF-1 function. Here we describe the use of peptide aptamer-based affinity chromatography coupled with mass spectrometry to define a multiprotein binding interface on IRF-1 (Mf2 domain; amino acids 106-140) and to identify Mf2-binding proteins from A375 cells. Based on their function as known transcriptional regulators, a selection of the Mf2 domain-binding proteins (NPM1, TRIM28, and YB-1) have been validated using in vitro and cell-based assays. Interestingly, although NPM1, TRIM28, and YB-1 all bind to the Mf2 domain, they have differing amino acid specificities, demonstrating the degree of combinatorial diversity and specificity available through linear interaction motifs.
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