Protein:protein interactions and the pairing of boundary elements in vivo.
Although it is now well-established that boundary elements/insulators function to subdivide eukaryotic chromosomes into autonomous regulatory domains, the underlying mechanisms remain elusive. One idea is that boundaries act as barriers, preventing the processive spreading of "active" or "silenced" chromatin between domains. Another is that the partitioning into autonomous functional units is a consequence of an underlying structural subdivision of the chromosome into higher order "looped" domains. In this view, boundaries are thought to delimit structural domains by interacting with each other or with some other nuclear structure. The studies reported here provide support for the looped domain model. We show that the Drosophila scs and scs' boundary proteins, Zw5 and BEAF, respectively, interact with each other in vitro and in vivo. Moreover, consistent with idea that this protein:protein interaction might facilitate pairing of boundary elements, we find that that scs and scs' are in close proximity to each other in Drosophila nuclei.
Blanton
Jason
J
Department of Molecular Biology, Princeton University, Princeton, New Jersey 08540, USA.
Gaszner
Miklos
M
Schedl
Paul
P
D000818:Animals; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D004330:Drosophila / Q000235:genetics* / Q000502:physiology; D029721:Drosophila Proteins / Q000235:genetics / Q000378:metabolism; D005136:Eye Proteins / Q000235:genetics / Q000378:metabolism; D066298:In Vitro Techniques; D038101:Insulator Elements / Q000502:physiology*; D009687:Nuclear Proteins / Q000378:metabolism; D011485:Protein Binding / Q000502:physiology
C452919:BEAF-32 protein, Drosophila; C108740:Chi protein, Drosophila; D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D005136:Eye Proteins; D009687:Nuclear Proteins; C121540:dwg protein, Drosophila; D004247:DNA