Multiple interactions are involved in a highly specific association of the Mod(mdg4)-67.2 isoform with the Su(Hw) sites in Drosophila
| Autor: | Pavel Georgiev, V. V. Molodina, Larisa Melnikova, M. V. Kostyuchenko, Anton Golovnin, Alexander Parshikov |
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| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Gene isoform Male Chromatin Immunoprecipitation Immunology Insulator (genetics) Biology Bioinformatics General Biochemistry Genetics and Molecular Biology 03 medical and health sciences CP190 Mod transcription factors Animals Drosophila Proteins Protein Isoforms Protein Interaction Domains and Motifs BTB domain Transcription factor lcsh:QH301-705.5 General Neuroscience Research digestive oral and skin physiology High-Throughput Nucleotide Sequencing FLYWCH domain Cell biology Chromatin chromatin insulators DNA-Binding Proteins 030104 developmental biology Phenotype lcsh:Biology (General) Genetic Loci Multiprotein Complexes Drosophila Insulator Elements Mod(mdg4) Research Article Protein Binding |
| Zdroj: | Open Biology Open Biology, Vol 7, Iss 10 (2017) |
| ISSN: | 2046-2441 |
| Popis: | The best-studiedDrosophilainsulator complex consists of two BTB-containing proteins, the Mod(mdg4)-67.2 isoform and CP190, which are recruited to the chromatin through interactions with the DNA-binding Su(Hw) protein. It was shown previously that Mod(mdg4)-67.2 is critical for the enhancer-blocking activity of the Su(Hw) insulators and it differs from more than 30 other Mod(mdg4) isoforms by the C-terminal domain required for a specific interaction with Su(Hw) only. The mechanism of the highly specific association between Mod(mdg4)-67.2 and Su(Hw) is not well understood. Therefore, we have performed a detailed analysis of domains involved in the interaction of Mod(mdg4)-67.2 with Su(Hw) and CP190. We found that the N-terminal region of Su(Hw) interacts with the glutamine-rich domain common to all the Mod(mdg4) isoforms. The unique C-terminal part of Mod(mdg4)-67.2 contains the Su(Hw)-interacting domain and the FLYWCH domain that facilitates a specific association between Mod(mdg4)-67.2 and the CP190/Su(Hw) complex. Finally, interaction between the BTB domain of Mod(mdg4)-67.2 and the M domain of CP190 has been demonstrated. By using transgenic lines expressing different protein variants, we have shown that all the newly identified interactions are to a greater or lesser extent redundant, which increases the reliability in the formation of the protein complexes. |
| Databáze: | OpenAIRE |
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