Journal article
An endogenous Suppressor of Hairy-wing insulator separates regulatory domains in Drosophila
Proceedings of the National Academy of Sciences - PNAS, Vol.100(23), pp.13436-13441
11/11/2003
DOI: 10.1073/pnas.2333111100
PMCID: PMC263832
PMID: 14597701
Abstract
Insulators define independent domains of gene function throughout the genome. The
Drosophila gypsy
insulator was isolated from the
gypsy
retrotransposon as a region that contains a cluster of binding sites for the Suppressor of Hairy-wing [Su(Hw)] protein. To study the effects of the
gypsy
insulator on gene expression within a single genomic domain, targeted gene replacement was used to exchange the endogenous
yellow
gene, located at cytological location 1A, with a set of
gypsy
-modified
yellow
genes. Replaced
yellow
genes carried a
gypsy
insulator positioned between the
yellow
promoter and either the upstream or the downstream tissue-specific enhancers. Whereas the
gypsy
insulator blocked the function of the upstream enhancers at the endogenous location, the downstream enhancers were not blocked. Investigation of the 1A region revealed two clustered Su(Hw)-binding sites downstream of the
yellow
gene, named 1A-2, that bind Su(Hw)
in vivo
and possess enhancer blocking function. We propose that interaction between 1A-2 and the
gypsy
insulator permits activation of
yellow
expression by enhancers in the neighboring
achaete
-
scute
complex, causing an apparent absence of the block of the downstream
yellow
enhancers. Based on these data, we suggest that 1A-2 is an endogenous Su(Hw) insulator that separates regulatory domains within the
Drosophila
genome.
Details
- Title: Subtitle
- An endogenous Suppressor of Hairy-wing insulator separates regulatory domains in Drosophila
- Creators
- Timothy J Parnell - Department of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242Michaela M Viering - Department of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242Astrid Skjesol - Department of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242Cecilia Helou - Department of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242Emily J Kuhn - Department of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242Pamela K Geyer - Department of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242
- Resource Type
- Journal article
- Publication Details
- Proceedings of the National Academy of Sciences - PNAS, Vol.100(23), pp.13436-13441
- DOI
- 10.1073/pnas.2333111100
- PMID
- 14597701
- PMCID
- PMC263832
- NLM abbreviation
- Proc Natl Acad Sci U S A
- ISSN
- 0027-8424
- eISSN
- 1091-6490
- Publisher
- National Academy of Sciences
- Language
- English
- Date published
- 11/11/2003
- Academic Unit
- Obstetrics and Gynecology; Biochemistry and Molecular Biology
- Record Identifier
- 9984025292502771
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