A multiprotein binding interface in an intrinsically disordered region of the tumour suppressor protein Interferon Regulatory Factor-1
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00209805%3A_____%2F11%3A%230000145" target="_blank" >RIV/00209805:_____/11:#0000145 - isvavai.cz</a>
Result on the web
<a href="http://www.jbc.org/content/286/16/14291.long" target="_blank" >http://www.jbc.org/content/286/16/14291.long</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1074/jbc.M110.204602" target="_blank" >10.1074/jbc.M110.204602</a>
Alternative languages
Result language
angličtina
Original language name
A multiprotein binding interface in an intrinsically disordered region of the tumour suppressor protein Interferon Regulatory Factor-1
Original language 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.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
FD - Oncology and haematology
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2011
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
The Journal of biological chemistry
ISSN
0021-9258
e-ISSN
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Volume of the periodical
286
Issue of the periodical within the volume
16
Country of publishing house
US - UNITED STATES
Number of pages
13
Pages from-to
14291-14303
UT code for WoS article
000289556200052
EID of the result in the Scopus database
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