title: Architectural proteins Pita, Zw5,and ZIPIC contain homodimerization domain and support specific long-range interactions in Drosophila.
abstract: According to recent models, as yet poorly studied architectural proteins appear to be required for local regulation of enhancer-promoter interactions, as well as for global chromosome organization. Transcription factors ZIPIC, Pita and Zw5 belong to the class of chromatin insulator proteins and preferentially bind to promoters near the TSS and extensively colocalize with cohesin and condensin complexes. ZIPIC, Pita and Zw5 are structurally similar in containing the N-terminal zinc finger-associated domain (ZAD) and different numbers of C2H2-type zinc fingers at the C-terminus. Here we have shown that the ZAD domains of ZIPIC, Pita and Zw5 form homodimers. In Drosophila transgenic lines, these proteins are able to support long-distance interaction between GAL4 activator and the reporter gene promoter. However, no functional interaction between binding sites for different proteins has been revealed, suggesting that such interactions are highly specific. ZIPIC facilitates long-distance stimulation of the reporter gene by GAL4 activator in yeast model system. Many of the genomic binding sites of ZIPIC, Pita and Zw5 are located at the boundaries of topologically associated domains (TADs). Thus, ZAD-containing zinc-finger proteins can be attributed to the class of architectural proteins.
authors.affiliation: Institute of Gene Biology, Russian Academy of Sciences, Vavilova str. 34/5, Moscow 119334, Russia.
authors.forename: Nikolay
authors.initials: N
authors.lastname: Zolotarev
authors.affiliation: Institute of Gene Biology, Russian Academy of Sciences, Vavilova str. 34/5, Moscow 119334, Russia.
authors.forename: Anna
authors.initials: A
authors.lastname: Fedotova
authors.affiliation: Institute of Gene Biology, Russian Academy of Sciences, Vavilova str. 34/5, Moscow 119334, Russia.
authors.forename: Olga
authors.initials: O
authors.lastname: Kyrchanova
authors.affiliation: Institute of Gene Biology, Russian Academy of Sciences, Vavilova str. 34/5, Moscow 119334, Russia.
authors.forename: Artem
authors.initials: A
authors.lastname: Bonchuk
authors.affiliation: Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119991, Russia; Institute for Information Transmission Problems, Russian Academy of Sciences, Moscow 127051 Russia; Department of Genetics, Faculty of Biology, Moscow State University, Moscow 119991, Russia.
authors.forename: Aleksey A
authors.initials: AA
authors.lastname: Penin
authors.affiliation: Moscow Institute of Physics and Technology (State University), Institutskiy per. 9, Dolgoprudny, Moscow Region 141700, Russia Vavilov Institute of General Genetics, Russian Academy of Sciences, Gubkina str. 3, Moscow, GSP-1, 119991, Russia.
authors.forename: Andrey S
authors.initials: AS
authors.lastname: Lando
authors.affiliation: Group of Protein Biosynthesis Regulation, Institute of Protein Research, Institutskaya str. 4, Pushchino 142290, Russia.
authors.forename: Irina A
authors.initials: IA
authors.lastname: Eliseeva
authors.affiliation: Vavilov Institute of General Genetics, Russian Academy of Sciences, Gubkina str. 3, Moscow, GSP-1, 119991, Russia Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilova str. 32, Moscow, GSP-1, 119991, Russia.
authors.forename: Ivan V
authors.initials: IV
authors.lastname: Kulakovskiy
authors.affiliation: Institute of Gene Biology, Russian Academy of Sciences, Vavilova str. 34/5, Moscow 119334, Russia maksog@mail.ru.
authors.forename: Oksana
authors.initials: O
authors.lastname: Maksimenko
authors.affiliation: Institute of Gene Biology, Russian Academy of Sciences, Vavilova str. 34/5, Moscow 119334, Russia georgiev_p@mail.ru.
authors.forename: Pavel
authors.initials: P
authors.lastname: Georgiev
mesh_terms: D000818:Animals; D030801:Animals, Genetically Modified; D001665:Binding Sites; D002460:Cell Line; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D029721:Drosophila Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000737:chemistry / Q000166:cytology / Q000196:embryology / Q000378:metabolism*; D005260:Female; D017930:Genes, Reporter / Q000235:genetics; D008297:Male; D011401:Promoter Regions, Genetic; D011485:Protein Binding; D000072417:Protein Domains; D055503:Protein Multimerization; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism; D013379:Substrate Specificity; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D019076:Transgenes / Q000235:genetics; D016335:Zinc Fingers
chemical_list: D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; C052130:GAL4 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; C000620216:ZIPIC protein, Drosophila; C121540:dwg protein, Drosophila; C507658:pita protein, Drosophila