Architectural protein Pita cooperates with dCTCF in organization of functional boundaries in Bithorax complex.

TitleArchitectural protein Pita cooperates with dCTCF in organization of functional boundaries in Bithorax complex.
Publication TypeJournal Article
Year of Publication2017
AuthorsKyrchanova, O, Zolotarev, N, Mogila, V, Maksimenko, O, Schedl, P, Georgiev, P
JournalDevelopment
Volume144
Issue14
Pagination2663-2672
Date Published2017 07 15
ISSN1477-9129
KeywordsAnimals, Animals, Genetically Modified, CCCTC-Binding Factor, Chromatin Immunoprecipitation, DNA-Binding Proteins, Drosophila melanogaster, Drosophila Proteins, Gene Expression Regulation, Developmental, Genes, Homeobox, Genes, Insect, Mutation, Protein Interaction Domains and Motifs, Repressor Proteins, Transcription Factors
Abstract

<p>Boundaries in the Bithorax complex (BX-C) of delimit autonomous regulatory domains that drive parasegment-specific expression of homeotic genes. BX-C boundaries have two crucial functions: they must block crosstalk between adjacent regulatory domains and at the same time facilitate boundary bypass. The C2H2 zinc-finger protein Pita binds to several BX-C boundaries, including and To study Pita functions, we have used a boundary replacement strategy by substituting modified DNAs for the boundary, which is located between the and regulatory domains. Multimerized Pita sites block crosstalk but fail to support regulation of (bypass). In the case of , we used a novel sensitized background to show that the two Pita-binding sites contribute to its boundary function. Although is from BX-C, it does not function appropriately when substituted for : it blocks crosstalk but does not support bypass. Mutation of the Pita site disrupts blocking activity and also eliminates dCTCF binding. In contrast, mutation of the dCTCF site does not affect Pita binding, and this mutant boundary retains partial function.</p>

DOI10.1242/dev.149815
Alternate JournalDevelopment
PubMed ID28619827
PubMed Central IDPMC5536930
Grant ListR01 GM043432 / GM / NIGMS NIH HHS / United States
R56 GM043432 / GM / NIGMS NIH HHS / United States