ArticleProceedings of the National Academy of Sciences of the United States of America2006
A structural role for ATP in the formation and stability of the human origin recognition complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 49 citations in OpenAlex.
- Reconstitution of human DNA licensing and the structural and functional analysis of key intermediates.Nature communications · 2025Article
- Proteome-wide mapping of short-lived proteins in human cells.Molecular cell · 2021Article
- HumanizedGenetics · 2020Article
- Structural insight into the assembly and conformational activation of human origin recognition complex.Cell discovery · 2020Article
- Conformational control and DNA-binding mechanism of the metazoan origin recognition complex.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Mechanisms and regulation of DNA replication initiation in eukaryotes.Critical reviews in biochemistry and molecular biology · 2017Review
- ORC interacts with THSC/TREX-2 and its subunits promote Nxf1 association with mRNP and mRNA export in Drosophila.Nucleic acids research · 2016Article
- Orc5 induces large-scale chromatin decondensation in a GCN5-dependent manner.Journal of cell science · 2016Article
- Drosophila model of Meier-Gorlin syndrome based on the mutation in a conserved C-Terminal domain of Orc6.American journal of medical genetics. Part A · 2015Article
- Orc1 Binding to Mitotic Chromosomes Precedes Spatial Patterning during G1 Phase and Assembly of the Origin Recognition Complex in Human Cells.The Journal of biological chemistry · 2015Article
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- Origin licensing requires ATP binding and hydrolysis by the MCM replicative helicase.Molecular cell · 2014Article
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- Regulating DNA replication in eukarya.Cold Spring Harbor perspectives in biology · 2013Review
- A structural framework for replication origin opening by AAA+ initiation factors.Current opinion in structural biology · 2013Review
- Mechanisms for initiating cellular DNA replication.Annual review of biochemistry · 2013Review
- Epstein-Barr nuclear antigen 1 (EBNA1)-dependent recruitment of origin recognition complex (Orc) on oriP of Epstein-Barr virus with purified proteins: stimulation by Cdc6 through its direct interaction with EBNA1.The Journal of biological chemistry · 2012Article
- Phosphorylation of ORC2 protein dissociates origin recognition complex from chromatin and replication origins.The Journal of biological chemistry · 2012Article
- The origin recognition complex: a biochemical and structural view.Sub-cellular biochemistry · 2012Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The locally restricted recruitment of the multisubunit origin recognition complex (ORC) to eukaryotic chromosomes defines the position of origins of DNA replication. In budding yeast and metazoans the DNA binding activity of ORC is stimulated by ATP and requires an AAA+-type nucleotide binding domain in the largest subunit. Little else is known about the mechanisms behind the ATP requirement for ORC in its initiator function and, specifically, the relevance of nucleotide binding domains present on other subunits. Here we show that ATP is required for specific subunit interactions in the human ORC, with the Orc4 subunit playing a critical role in this dynamic process. ATP is essential for the maintenance of ORC integrity and facilitates complex formation. Thus, besides its previously identified role in DNA binding, ATP serves also as a structural cofactor for human ORC.
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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.