ArticleProceedings of the National Academy of Sciences of the United States of America1996
The Drosophila melanogaster dodo (dod) gene, conserved in humans, is functionally interchangeable with the ESS1 cell division gene of Saccharomyces cerevisiae.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 108 citations in OpenAlex.
- Article
- Article
- Pin1 and Alzheimer's disease.Translational research : the journal of laboratory and clinical medicine · 2023Review
- Coevolution of the Ess1-CTD axis in polar fungi suggests a role for phase separation in cold tolerance.Science advances · 2022Article
- The kingdom of the prolyl-isomerase Pin1: The structural and functional convergence and divergence of Pin1.Frontiers in cell and developmental biology · 2022Review
- Structures of tweety homolog proteins TTYH2 and TTYH3 reveal a CaNature communications · 2021Article
- Cryo-EM structures of the TTYH family reveal a novel architecture for lipid interactions.Nature communications · 2021Article
- Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism.Communications biology · 2021Article
- Oncogenic Hijacking of the PIN1 Signaling Network.Frontiers in oncology · 2019Review
- Phosphorylation induces sequence-specific conformational switches in the RNA polymerase II C-terminal domain.Nature communications · 2017Article
- The Ess1 prolyl isomerase: traffic cop of the RNA polymerase II transcription cycle.Biochimica et biophysica acta · 2014Review
- Multiple roles for the Ess1 prolyl isomerase in the RNA polymerase II transcription cycle.Molecular and cellular biology · 2012Article
- Characteristics and evolution of the PUF gene family in Bombyx mori and 27 other species.Molecular biology reports · 2012Article
- The ubiquitin-protein ligase Nedd4-2 differentially interacts with and regulates members of the Tweety family of chloride ion channels.The Journal of biological chemistry · 2008Article
- The WW domain protein PRO40 is required for fungal fertility and associates with Woronin bodies.Eukaryotic cell · 2007Article
- Identification and comparative analysis of sixteen fungal peptidyl-prolyl cis/trans isomerase repertoires.BMC genomics · 2006Article
- The structure of the Candida albicans Ess1 prolyl isomerase reveals a well-ordered linker that restricts domain mobility.Biochemistry · 2005Article
- Identification and comparative analysis of the peptidyl-prolyl cis/trans isomerase repertoires of H. sapiens, D. melanogaster, C. elegans, S. cerevisiae and Sz. pombe.Comparative and functional genomics · 2005Article
- Immunophilins and parvulins. Superfamily of peptidyl prolyl isomerases in Arabidopsis.Plant physiology · 2004Article
- Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have sequenced the region of DNA adjacent to and including the flightless (fli) gene of Drosophila melanogaster and molecularly characterized four transcription units within it, which we have named tweety (twe), flightless (fli), dodo (dod), and penguin (pen). We have performed deletion and transgenic analysis to determine the consequences of the quadruple gene removal. Only the flightless gene is vital to the organism; the simultaneous absence of the other three allows the overriding majority of individuals to develop to adulthood and to fly normally. These gene deletion results are evaluated in the context of the redundancy and degeneracy inherent in many genetic networks. Our cDNA analyses and data-base searches reveal that the predicted dodo protein has homologs in other eukaryotes and that it is made up of two different domains. The first, designated WW, is involved in protein-protein interactions and is found in functionally diverse proteins including human dystrophin. The second is involved in accelerating protein folding and unfolding and is found in Escherichia coli in a new family of peptidylprolyl cis-trans isomerases (PPIases; EC 5.2.1.8). In eukaryotes, PPIases occur in the nucleus and the cytoplasm and can form stable associations with transcription factors, receptors, and kinases. Given this particular combination of domains, the dodo protein may well participate in a multisubunit complex involved in the folding and activation of signaling molecules. When we expressed the dodo gene product in Saccharomyces cerevisiae, it rescued the lethal phenotype of the ESS1 cell division gene.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.