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

J 2023

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

HOUSER, Josef, Kristína JENDRUCHOVÁ, Andrea KNIGHT a Martin PISKÁČEK

Základní údaje

Originální název

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

Autoři

HOUSER, Josef (203 Česká republika, domácí), Kristína JENDRUCHOVÁ (703 Slovensko, domácí), Andrea KNIGHT (203 Česká republika, domácí) a Martin PISKÁČEK (40 Rakousko, garant, domácí)

Vydání

The Biochemical journal, LONDON, PORTLAND PRESS LTD, 2023, 0264-6021

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

30102 Immunology

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 4.100 v roce 2022

Kód RIV

RIV/00216224:14110/23:00130376

Organizační jednotka

Lékařská fakulta

DOI

http://dx.doi.org/10.1042/BCJ20220605

UT WoS

000950074500001

Klíčová slova anglicky

CPB; 9aaTAD; Transcription

Štítky

14110224, 14110518, CF BIC, CF NMR, CF PROT, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 18. 10. 2024 15:48, Ing. Marie Švancarová

Anotace

V originále

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.

Návaznosti

LM2018127, projekt VaV

Název: Česká infrastruktura pro integrativní strukturní biologii (Akronym: CIISB)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Czech Infrastructure for Integrative Structural Biology

NV19-05-00410, projekt VaV

Název: Úloha cytotoxických gamma-delta T buněk na terapeutické rezistenci a recidivě Glioblastoma Multiforme

Investor: Ministerstvo zdravotnictví ČR, Úloha cytotoxických gamma-delta T buněk na terapeutické rezistenci a recidivě Glioblastoma Multiforme

90127, velká výzkumná infrastruktura

Název: CIISB II

Citovat

HOUSER, Josef, Kristína JENDRUCHOVÁ, Andrea KNIGHT a Martin PISKÁČEK. The NFkB activation domain is 14-amino-acid-long variant of the 9aaTAD. The Biochemical journal. LONDON: PORTLAND PRESS LTD, 2023, roč. 480, č. 5, s. 297-306. ISSN 0264-6021. Dostupné z: https://dx.doi.org/10.1042/BCJ20220605.

@article{2261797,
   author = {Houser, Josef and Jendruchová, Kristína and Knight, Andrea and Piskáček, Martin},
   article_location = {LONDON},
   article_number = {5},
   doi = {http://dx.doi.org/10.1042/BCJ20220605},
   keywords = {CPB; 9aaTAD; Transcription},
   language = {eng},
   issn = {0264-6021},
   journal = {The Biochemical journal},
   title = {The NFkB activation domain is 14-amino-acid-long variant of the 9aaTAD},
   url = {https://portlandpress.com/biochemj/article/doi/10.1042/BCJ20220605/232597/The-NFkB-activation-domain-is-14-amino-acid-long},
   volume = {480},
   year = {2023}
}

TY  - JOUR
ID  - 2261797
AU  - Houser, Josef - Jendruchová, Kristína - Knight, Andrea - Piskáček, Martin
PY  - 2023
TI  - The NFkB activation domain is 14-amino-acid-long variant of the 9aaTAD
JF  - The Biochemical journal
VL  - 480
IS  - 5
SP  - 297-306
EP  - 297-306
PB  - PORTLAND PRESS LTD
SN  - 02646021
KW  - CPB
KW  - 9aaTAD
KW  - Transcription
UR  - https://portlandpress.com/biochemj/article/doi/10.1042/BCJ20220605/232597/The-NFkB-activation-domain-is-14-amino-acid-long
N2  - 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.
ER  -

HOUSER, Josef, Kristína JENDRUCHOVÁ, Andrea KNIGHT a Martin PISKÁČEK. The NFkB activation domain is 14-amino-acid-long variant of the 9aaTAD. \textit{The Biochemical journal}. LONDON: PORTLAND PRESS LTD, 2023, roč.~480, č.~5, s.~297-306. ISSN~0264-6021. Dostupné z: https://dx.doi.org/10.1042/BCJ20220605.

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