ArticleThe Journal of biological chemistry2012
Crystal structure of elongator subcomplex Elp4-6.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 43 citations in OpenAlex.
- A common variant in the CLDN7/ELP5 locus predicts adiponectin change with lifestyle intervention and improved fitness in obese individuals with diabetes.Physiological genomics · 2015Trial
- TaELP2 Interacts With TaDCL1 and Negatively Regulates Wheat Resistance Against Stripe Rust.Molecular plant pathology · 2026Article
- Evolutionary Conservation in Protein-Protein Interactions and Structures of the Elongator Sub-Complex ELP456 fromInternational journal of molecular sciences · 2024Article
- Cryo-EM structure of the fully assembled Elongator complex.Nucleic acids research · 2023Article
- Insights into the Bioinformatics and Transcriptional Analysis of the Elongator Complexes (Plants (Basel, Switzerland) · 2023Article
- Wheat Elongator Subunit 4 Negatively Regulates Freezing Tolerance by Regulating Ethylene Accumulation.International journal of molecular sciences · 2022Article
- Biochemical and Structural Characterization of Human Core Elongator and Its Subassemblies.ACS omega · 2022Article
- Candidate Markers of Olaparib Response from Genomic Data Analyses of Human Cancer Cell Lines.Cancers · 2021Article
- Plant Elongator-Protein Complex of Diverse Activities Regulates Growth, Development, and Immune Responses.International journal of molecular sciences · 2020Review
- Eukaryotic life without tQCUG: the role of Elongator-dependent tRNA modifications in Dictyostelium discoideum.Nucleic acids research · 2020Article
- Alkyladenine DNA glycosylase associates with transcription elongation to coordinate DNA repair with gene expression.Nature communications · 2019Article
- Structural insights into the function of Elongator.Cellular and molecular life sciences : CMLS · 2018Review
- TheFrontiers in plant science · 2018Article
- Development of an in silico method for the identification of subcomplexes involved in the biogenesis of multiprotein complexes in Saccharomyces cerevisiae.BMC systems biology · 2017Article
- Architecture of the yeast Elongator complex.EMBO reports · 2017Article
- Molecular architecture of the yeast Elongator complex reveals an unexpected asymmetric subunit arrangement.EMBO reports · 2017Article
- Structural basis for tRNA modification by Elp3 from Dehalococcoides mccartyi.Nature structural & molecular biology · 2016Article
- The Many Faces of Elongator in Neurodevelopment and Disease.Frontiers in molecular neuroscience · 2016Review
- Dimerization of elongator protein 1 is essential for Elongator complex assembly.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Meta-regulation of Arabidopsis auxin responses depends on tRNA maturation.Cell reports · 2015Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Elongator is a multiprotein complex composed of two subcomplexes, Elp1-3 and Elp4-6. Elongator is highly conserved between yeast and humans and plays an important role in RNA polymerase II-mediated transcriptional elongation and many other processes, including cytoskeleton organization, exocytosis, and tRNA modification. Here, we determined the crystal structure of the Elp4-6 subcomplex of yeast. The overall structure of Elp4-6 revealed that Elp6 acts as a bridge to assemble Elp4 and Elp5. Detailed structural and sequence analyses revealed that each subunit in the Elp4-6 subcomplex forms a RecA-ATPase-like fold, although it lacks the key sequence signature of ATPases. Site-directed mutagenesis and biochemical analyses indicated that the Elp4-6 subcomplex can assemble into a hexameric ring-shaped structure in vitro and in vivo. Furthermore, GST pulldown assays showed that the ring-shaped assembly of the Elp4-6 subcomplex is important for its specific histone H3 binding. Our results may shed light on the substrate recognition and assembly of the holo-Elongator complex.
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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.