About: A multiprotein binding interface in an intrinsically disordered region of the tumour suppressor protein Interferon Regulatory Factor-1     Goto   Sponge   NotDistinct   Permalink

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Description
  • The interferon-regulated transcription factor IRF-1 is predicted to be largely disordered outside of the DNA-binding domain. 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. 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.
  • The interferon-regulated transcription factor IRF-1 is predicted to be largely disordered outside of the DNA-binding domain. 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. 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. (en)
Title
  • A multiprotein binding interface in an intrinsically disordered region of the tumour suppressor protein Interferon Regulatory Factor-1
  • A multiprotein binding interface in an intrinsically disordered region of the tumour suppressor protein Interferon Regulatory Factor-1 (en)
skos:prefLabel
  • A multiprotein binding interface in an intrinsically disordered region of the tumour suppressor protein Interferon Regulatory Factor-1
  • A multiprotein binding interface in an intrinsically disordered region of the tumour suppressor protein Interferon Regulatory Factor-1 (en)
skos:notation
  • RIV/00209805:_____/11:#0000145!RIV12-MSM-00209805
http://linked.open...avai/predkladatel
http://linked.open...avai/riv/aktivita
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  • P(ED2.1.00/03.0101), P(GAP304/10/0868), P(LC07017), Z(AV0Z50200510), Z(MO0FVZ0000604)
http://linked.open...iv/cisloPeriodika
  • 16
http://linked.open...vai/riv/dodaniDat
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  • 183917
http://linked.open...ai/riv/idVysledku
  • RIV/00209805:_____/11:#0000145
http://linked.open...riv/jazykVysledku
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  • IRF-1; Mf2 domain; YB-1; TRIM28 (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [52D1B03F3189]
http://linked.open...i/riv/nazevZdroje
  • The Journal of biological chemistry
http://linked.open...in/vavai/riv/obor
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http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 286
http://linked.open...iv/tvurceVysledku
  • Vojtěšek, Bořivoj
http://linked.open...ain/vavai/riv/wos
  • 000289556200052
http://linked.open...n/vavai/riv/zamer
issn
  • 0021-9258
number of pages
http://bibframe.org/vocab/doi
  • 10.1074/jbc.M110.204602
is http://linked.open...avai/riv/vysledek of
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