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Universal two-point interaction of mediator KIX with 9aaTAD activation domains

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F65269705%3A_____%2F21%3A00075355" target="_blank" >RIV/65269705:_____/21:00075355 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216224:14110/21:00120140

  • Result on the web

    <a href="https://onlinelibrary.wiley.com/doi/10.1002/jcb.30075" target="_blank" >https://onlinelibrary.wiley.com/doi/10.1002/jcb.30075</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/jcb.30075" target="_blank" >10.1002/jcb.30075</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Universal two-point interaction of mediator KIX with 9aaTAD activation domains

  • Original language description

    The nine-amino-acid activation domain (9aaTAD) is defined by a short amino acid pattern including two hydrophobic regions (positions p3-4 and p6-7). The KIX domain of mediator transcription CBP interacts with the 9aaTAD domains of transcription factors MLL, E2A, NF-kB, and p53. In this study, we analyzed the 9aaTADs-KIX interactions by nuclear magnetic resonance. The positions of three KIX helixes alpha 1-alpha 2-alpha 3 are influenced by sterically-associated hydrophobic I611, L628, and I660 residues that are exposed to solvent. The positions of two rigid KIX helixes alpha 1 and alpha 2 generate conditions for structural folding in the flexible KIX-L12-G2 regions localized between them. The three KIX I611, L628, and I660 residues interact with two 9aaTAD hydrophobic residues in positions p3 and p4 and together build a hydrophobic core of five residues (5R). Numerous residues in 9aaTAD position p3 and p4 could provide this interaction. Following binding of the 9aaTAD to KIX, the hydrophobic I611, L628, and I660 residues are no longer exposed to solvent and their position changes inside the hydrophobic core together with position of KIX alpha 1-alpha 2-alpha 3 helixes. The new positions of the KIX helixes alpha 1 and alpha 2 allow the KIX-L12-G2 enhanced formation. The second hydrophobic region of the 9aaTAD (positions p6 and p7) provides strong binding with the KIX-L12-G2 region. Similarly, multiple residues in 9aaTAD position p6 and p7 could provide this interaction. In conclusion, both 9aaTAD regions p3, p4 and p6, p7 provide co-operative and highly universal binding to mediator KIX. The hydrophobic core 5R formation allows new positions of the rigid KIX alpha-helixes and enables the enhanced formation of the KIX-L12-G2 region. This contributes to free energy and is the key for the KIX-9aaTAD binding. Therefore, the 9aaTAD-KIX interactions do not operate under the rigid key-and-lock mechanism what explains the 9aaTAD natural variability.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    30200 - Clinical medicine

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

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

Others

  • Publication year

    2021

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Journal of Cellular Biochemistry

  • ISSN

    0730-2312

  • e-ISSN

  • Volume of the periodical

    122

  • Issue of the periodical within the volume

    10

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    12

  • Pages from-to

    1544-1555

  • UT code for WoS article

    000669605600001

  • EID of the result in the Scopus database

    2-s2.0-85109188946