A multiprotein binding interface in an intrinsically disordered region of the tumour suppressor protein Interferon Regulatory Factor-1

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

A multiprotein binding interface in an intrinsically disordered region of the tumour suppressor protein Interferon Regulatory Factor-1

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

A multiprotein binding interface in an intrinsically disordered region of the tumour suppressor protein Interferon Regulatory Factor-1

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

FD - Onkologie a hematologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2011

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

The Journal of biological chemistry

ISSN

0021-9258

e-ISSN

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Svazek periodika

286

Číslo periodika v rámci svazku

16

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

13

Strana od-do

14291-14303

Kód UT WoS článku

000289556200052

EID výsledku v databázi Scopus

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