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 and Martin PISKÁČEK

Basic information

Original name

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

Authors

HOUSER, Josef (203 Czech Republic, belonging to the institution), Kristína JENDRUCHOVÁ (703 Slovakia, belonging to the institution), Andrea KNIGHT (203 Czech Republic, belonging to the institution) and Martin PISKÁČEK (40 Austria, guarantor, belonging to the institution)

Edition

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

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

30102 Immunology

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 4.100 in 2022

RIV identification code

RIV/00216224:14110/23:00130376

Organization unit

Faculty of Medicine

DOI

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

UT WoS

000950074500001

Keywords in English

CPB; 9aaTAD; Transcription

Abstract

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.

Links

NV19-05-00410, research and development project

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

Investor: Ministry of Health of the CR

90127, large research infrastructures

Name: CIISB II

Citovat

HOUSER, Josef, Kristína JENDRUCHOVÁ, Andrea KNIGHT and Martin PISKÁČEK. The NFkB activation domain is 14-amino-acid-long variant of the 9aaTAD. The Biochemical journal. LONDON: PORTLAND PRESS LTD, 2023, vol. 480, No 5, p. 297-306. ISSN 0264-6021. Available from: 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 and Martin PISKÁČEK. The NFkB activation domain is 14-amino-acid-long variant of the 9aaTAD. \textit{The Biochemical journal}. LONDON: PORTLAND PRESS LTD, 2023, vol.~480, No~5, p.~297-306. ISSN~0264-6021. Available from: https://dx.doi.org/10.1042/BCJ20220605.

Detailed Information on Publication Record