The NFkB activation domain is 14-amino-acid-long variant of the 9aaTAD

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14110%2F23%3A00130376" target="_blank" >RIV/00216224:14110/23:00130376 - isvavai.cz</a>

Výsledek na webu

<a href="https://portlandpress.com/biochemj/article/doi/10.1042/BCJ20220605/232597/The-NFkB-activation-domain-is-14-amino-acid-long" target="_blank" >https://portlandpress.com/biochemj/article/doi/10.1042/BCJ20220605/232597/The-NFkB-activation-domain-is-14-amino-acid-long</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1042/BCJ20220605" target="_blank" >10.1042/BCJ20220605</a>

Jazyk výsledku

angličtina

Název v původním jazyce

The NFkB activation domain is 14-amino-acid-long variant of the 9aaTAD

Popis výsledku v původním jazyce

The nine-amino-acid TransActivation Domains (9aaTAD) was identified in numerous transcription factors including Gal4, p53, E2A, MLL, c-Myc, N-Myc, and also in SP, KLF and SOX families. Most of the 9aaTAD domains interact with the KIX domain of transcription mediators MED15 and CBP to activate transcription. The NFkB activation domain occupied the same position on the KIX domain as the 9aaTADs of MLL, E2A and p53. Binding of the KIX domain is established by the two-point interaction involving 9aaTAD positions p3-4 and p6-7. The NFkB primary binding region (position p3-4) is almost identical to MLL and E2A, but secondary NFkB binding region differs by the position and engages the distal NFkB region p10-11. Thus, the NFkB activation domain is 5 amino acids longer than the other 9aaTADs. The NFkB activation domain includes an additional region, which we called the Omichinski Insert extending activation domain length to 14 amino acids. By deletion, we demonstrated that Omichinski Insert is an entirely non-essential part of NFkB activation domain. In summary, we recognized the NFkB activation domain as prolonged 9aaTAD conserved in evolution from humans to amphibians.

Název v anglickém jazyce

The NFkB activation domain is 14-amino-acid-long variant of the 9aaTAD

Popis výsledku anglicky

The nine-amino-acid TransActivation Domains (9aaTAD) was identified in numerous transcription factors including Gal4, p53, E2A, MLL, c-Myc, N-Myc, and also in SP, KLF and SOX families. Most of the 9aaTAD domains interact with the KIX domain of transcription mediators MED15 and CBP to activate transcription. The NFkB activation domain occupied the same position on the KIX domain as the 9aaTADs of MLL, E2A and p53. Binding of the KIX domain is established by the two-point interaction involving 9aaTAD positions p3-4 and p6-7. The NFkB primary binding region (position p3-4) is almost identical to MLL and E2A, but secondary NFkB binding region differs by the position and engages the distal NFkB region p10-11. Thus, the NFkB activation domain is 5 amino acids longer than the other 9aaTADs. The NFkB activation domain includes an additional region, which we called the Omichinski Insert extending activation domain length to 14 amino acids. By deletion, we demonstrated that Omichinski Insert is an entirely non-essential part of NFkB activation domain. In summary, we recognized the NFkB activation domain as prolonged 9aaTAD conserved in evolution from humans to amphibians.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

30102 - Immunology

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

2023

Kód důvěrnosti údajů

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

Název periodika

The Biochemical journal

ISSN

0264-6021

e-ISSN

1470-8728

Svazek periodika

480

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

10

Strana od-do

297-306

Kód UT WoS článku

000950074500001

EID výsledku v databázi Scopus

2-s2.0-85150001300