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Study of the N-Terminal Domain Homodimerization in Human Proteins with Zinc Finger Clusters

CTCF belongs to a large family of transcription factors with clusters of C2H2-type zinc finger domains (C2H2 proteins) and is a main architectural protein in mammals. Human CTCF has a homodimerizing unstructured domain at the N-terminus which is involved in long-distance interactions. To test the pr...

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Detalles Bibliográficos
Autores principales: Fursenko, D. V., Georgiev, P. G., Bonchuk, A. N.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Pleiades Publishing 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8382608/
https://www.ncbi.nlm.nih.gov/pubmed/34426923
http://dx.doi.org/10.1134/S1607672921040050
Descripción
Sumario:CTCF belongs to a large family of transcription factors with clusters of C2H2-type zinc finger domains (C2H2 proteins) and is a main architectural protein in mammals. Human CTCF has a homodimerizing unstructured domain at the N-terminus which is involved in long-distance interactions. To test the presence of similar N-terminal domains in other human C2H2 proteins, a yeast two-hybrid system was used. In total, the ability of unstructured N-terminal domains to homodimerize was investigated for six human C2H2 proteins with an expression profile similar to CTCF. The data indicate the lack of the homodimerization ability of these domains. On the other hand, three C2H2 proteins containing the structured domain DUF3669 at the N-terminus demonstrated homo- and heterodimerization activity.