ArticleMolecular and cellular biology1997
Two types of zinc fingers are required for dimerization of the serendipity delta transcriptional activator.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 31 citations in OpenAlex.
- Decoding the molecular logic of rapidly evolving ZAD zinc finger proteins inScience advances · 2026Article
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- Structure of Arabidopsis HISTONE DEACETYLASE15.Plant physiology · 2020Article
- Article
- Architectural proteins Pita, Zw5,and ZIPIC contain homodimerization domain and support specific long-range interactions in Drosophila.Nucleic acids research · 2016Article
- An efficient and cost-effective protocol for selecting transcription factor binding sites that reduces isotope usage.Journal of biomolecular techniques : JBT · 2012Article
- The Drosophila zinc finger protein trade embargo is required for double strand break formation in meiosis.PLoS genetics · 2011Article
- Protease activity, self interaction, and small interfering RNA binding of the silencing suppressor p1b from cucumber vein yellowing ipomovirus.Journal of virology · 2008Article
- Screens for piwi suppressors in Drosophila identify dosage-dependent regulators of germline stem cell division.Genetics · 2003Article
- Genomic expansion and clustering of ZAD-containing C2H2 zinc-finger genes in Drosophila.EMBO reports · 2002Article
- Identification of DNA recognition sequences and protein interaction domains of the multiple-Zn-finger protein Roaz.Molecular and cellular biology · 1998Article
- ZAD-Domain Is Essential for Nuclear Localization of Insulator Proteins in Drosophila melanogaster.Acta naturaeArticle
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The serendipity (sry) delta zinc finger protein controls bicoid gene expression during Drosophila melanogaster oogenesis. In addition, sry delta mutants display various zygotic phenotypes, ranging from abnormal embryogenesis to sex-biased adult lethality. We report here that sry delta is a sequence-specific transcriptional activator. A single sry delta consensus binding site (SDCS), in either orientation, is sufficient to promote transcription activation in cell culture, and multiple SDCSs mediate a strong synergistic activation, reflecting the cooperativity of sry delta binding to DNA. Further, several lines of evidence strongly suggest that sry delta binds to DNA as a dimer. While each of three point mutations located in the third zinc finger of sry delta drastically reduces its DNA binding affinity, a fourth mutation, located in the N-terminal region of the protein, specifically affects the cooperativity of DNA binding. This mutation reveals the functional importance of a putative Cys2/Cys2 zinc finger motif of a novel type, located outside the DNA binding domain. A systematic deletion analysis shows that interaction between this proposed Cys2/Cys2 motif and a classical Cys2/His2 zinc finger mediates homodimerization, which is required for DNA binding cooperativity.
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