title: Chromatin domain boundaries in the Bithorax complex.
abstract: Eukaryotic chromosomes are thought to be organized into a series of discrete higher-order chromatin domains. This organization is believed to be important not only in the compaction of the chromatin fibre, but also in the utilization of genetic information. Critical to this model are the domain boundaries that delimit and segregate the chromosomes into units of independent gene activity. In Drosophila, such domain boundaries have been identified through two different approaches. On the one hand, elements like scs/scs' and the reiterated binding site for the SU(HW) protein have been characterized through their activity of impeding enhancer-promoter interactions when intercalated between them. Their role of chromatin insulators can protect transgenes from genomic position effects, thereby establishing independent functional domains within the chromosome. On the other hand, domain boundaries of the Bithorax complex (BX-C) like Fab-7 and Mcp have been identified through mutational analysis. Mcp and Fab-7, however, may represent a specific class of boundary elements; instead of separating adjacent domains that contain separate structural genes. Mcp and Fab-7 delimit adjacent cis-regulatory domains, each of which interacts independently with their target promoters. In this article, we review the genetic and molecular characteristics of the domain boundaries of the BX-C. We describe how Fab-7 functions to confine activating as well as repressive signals to the flanking regulatory domains. Although the mechanisms by which Fab-7 works as a domain boundary remain an open issue, we provide preliminary evidence that Fab-7 is not a mere insulator like scs or the reiterated binding site for the SU(HW) protein.
authors.affiliation: Department of Zoology and Animal Biology, University of Geneva, Switzerland.
authors.forename: J
authors.initials: J
authors.lastname: Mihaly
authors.forename: I
authors.initials: I
authors.lastname: Hogga
authors.forename: S
authors.initials: S
authors.lastname: Barges
authors.forename: M
authors.initials: M
authors.lastname: Galloni
authors.forename: R K
authors.initials: RK
authors.lastname: Mishra
authors.forename: K
authors.initials: K
authors.lastname: Hagstrom
authors.forename: M
authors.initials: M
authors.lastname: Müller
authors.forename: P
authors.initials: P
authors.lastname: Schedl
authors.forename: L
authors.initials: L
authors.lastname: Sipos
authors.forename: J
authors.initials: J
authors.lastname: Gausz
authors.forename: H
authors.initials: H
authors.lastname: Gyurkovics
authors.forename: F
authors.initials: F
authors.lastname: Karch
mesh_terms: D000818:Animals; D002843:Chromatin / Q000737:chemistry* / Q000235:genetics; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics*; D004330:Drosophila / Q000235:genetics*; D029721:Drosophila Proteins; D018398:Homeodomain Proteins / Q000737:chemistry / Q000235:genetics*; D019476:Insect Proteins / Q000737:chemistry / Q000235:genetics*; D009687:Nuclear Proteins; D017434:Protein Structure, Tertiary; D014157:Transcription Factors
chemical_list: C062393:Abd-B proteins, Drosophila; D002843:Chromatin; D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D018398:Homeodomain Proteins; D019476:Insect Proteins; D009687:Nuclear Proteins; D014157:Transcription Factors; C066177:Ubx protein, Drosophila; C066591:abd-A protein, Drosophila