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|Title:||The extrachromosomal EAST protein of drosophila can associate with polytene chromosomes and regulate gene expression|
|Authors:||Wasser, M. |
|Citation:||Wasser, M., Chia, W. (2007-05-02). The extrachromosomal EAST protein of drosophila can associate with polytene chromosomes and regulate gene expression. PLoS ONE 2 (5) : -. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0000412|
|Abstract:||The EAST protein of Drosophila is a component of an expandable extrachromosomal domain of the nucleus. To better understand its function, we studied the dynamics and localization of GFP-tagged EAST. In live larval salivary glands, EAST-GFP is highly mobile and localizes to the extrachromosomal nucleoplasm. When these cells are permeabilized, EAST-GFP rapidly associated with polytene chromosomes. The affinity to chromatin increases and mobility decreases with decreasing salt concentration. Deleting the C-terminal residues 1535 to 2301 of EAST strongly reduces the affinity to polytene chromosomes. The bulk of EAST-GFP co-localizes with heterochromatin and is absent from transcriptionally active chromosomal regions. The predominantly chromosomal localization of EAST-GFP can be detected in non-detergent treated salivary glands of pupae as they undergo apoptosis, however not in earlier stages of development. Consistent with this chromosomal pattern of localization, genetic evidence indicates a role for EAST in the repression of gene expression, since a lethal east mutation is allelic to the viable mutation suppressor of white-spotted. We propose that EAST acts as an ion sensor that modulates gene expression in response to changing intracellular ion concentrations. © 2007 Wasser, Chia.|
|Source Title:||PLoS ONE|
|Appears in Collections:||Staff Publications|
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