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

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.

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

• Original language: English
• Type of outcome: Article in a journal
• Field of Study: 30102 Immunology
• Country of publisher: United Kingdom of Great Britain and Northern Ireland
• Confidentiality degree: is not subject to a state or trade secret
• WWW: 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
• Tags: 14110224, 14110518, CF BIC, CF NMR, CF PROT, rivok
• Tags: International impact, Reviewed

Abstract

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

• LM2018127, research and development project: Name: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB)

Investor: Ministry of Education, Youth and Sports of the CR

• 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

• 90242, large research infrastructures: Name: CIISB III