ArticleThe Journal of biological chemistry2011
Enabling association of the GINS protein tetramer with the mini chromosome maintenance (Mcm)2-7 protein complex by phosphorylated Sld2 protein and single-stranded origin DNA.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 34 citations in OpenAlex.
- Sld3CBD-Cdc45 structural insights into Cdc45 recruitment for CMG complex formation during DNA replication.eLife · 2025Article
- An intact Mcm10 coiled-coil interaction surface is important for origin melting, helicase assembly and the recruitment of Pol-α to Mcm2-7.Nucleic acids research · 2017Article
- Yeast Hrq1 shares structural and functional homology with the disease-linked human RecQ4 helicase.Nucleic acids research · 2017Article
- Mechanisms and regulation of DNA replication initiation in eukaryotes.Critical reviews in biochemistry and molecular biology · 2017Review
- A Positive Amplification Mechanism Involving a Kinase and Replication Initiation Factor Helps Assemble the Replication Fork Helicase.The Journal of biological chemistry · 2017Article
- Article
- An Mcm10 Mutant Defective in ssDNA Binding Shows Defects in DNA Replication Initiation.Journal of molecular biology · 2016Article
- TIMELESS Suppresses the Accumulation of Aberrant CDC45·MCM2-7·GINS Replicative Helicase Complexes on Human Chromatin.The Journal of biological chemistry · 2016Article
- Structural and biochemical characterization of an RNA/DNA binding motif in the N-terminal domain of RecQ4 helicases.Scientific reports · 2016Article
- Mcm10 coordinates the timely assembly and activation of the replication fork helicase.Nucleic acids research · 2016Article
- Interaction of RECQ4 and MCM10 is important for efficient DNA replication origin firing in human cells.Oncotarget · 2015Article
- The Replication Initiation Protein Sld3/Treslin Orchestrates the Assembly of the Replication Fork Helicase during S Phase.The Journal of biological chemistry · 2015Article
- Dpb11 protein helps control assembly of the Cdc45·Mcm2-7·GINS replication fork helicase.The Journal of biological chemistry · 2015Article
- Switch on the engine: how the eukaryotic replicative helicase MCM2-7 becomes activated.Chromosoma · 2015Review
- The Dbf4-Cdc7 kinase promotes Mcm2-7 ring opening to allow for single-stranded DNA extrusion and helicase assembly.The Journal of biological chemistry · 2015Article
- The intrinsically disordered amino-terminal region of human RecQL4: multiple DNA-binding domains confer annealing, strand exchange and G4 DNA binding.Nucleic acids research · 2014Article
- The replication initiation protein Sld2 regulates helicase assembly.The Journal of biological chemistry · 2014Article
- Cdc45 protein-single-stranded DNA interaction is important for stalling the helicase during replication stress.The Journal of biological chemistry · 2013Article
- The N-terminus of the human RecQL4 helicase is a homeodomain-like DNA interaction motif.Nucleic acids research · 2012Article
- The interaction networks of the budding yeast and human DNA replication-initiation proteins.Cell cycle (Georgetown, Tex.)Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Cdc45-Mcm2-7-GINS (CMG) complex is the replication fork helicase in eukaryotes. Synthetic lethal with Dpb11-1 (Sld2) is required for the initiation of DNA replication, and the S phase cyclin-dependent kinase (S-CDK) phosphorylates Sld2 in vivo. We purified components of the replication initiation machinery and studied their interactions in vitro. We found that unphosphorylated or CDK-phosphorylated Sld2 binds to the mini chromosome maintenance (Mcm)2-7 complex with similar efficiency. Sld2 interaction with Mcm2-7 blocks the interaction between GINS and Mcm2-7. The interaction between CDK-phosphorylated Sld2 and Mcm2-7 is substantially inhibited by origin single-stranded DNA (ssDNA). Furthermore, origin ssDNA allows GINS to bind to Mcm2-7 in the presence of CDK-phosphorylated Sld2. However, unphosphorylated Sld2 blocks the interaction between GINS and Mcm2-7 even in the presence of origin ssDNA. We identified a mutant of Sld2 that does not bind to DNA. When this mutant is expressed in yeast cells, cell growth is severely inhibited with very slow progression into S phase. We propose a model wherein Sld2 blocks the interaction between GINS and Mcm2-7 in vivo. Once origin ssDNA is extruded from the Mcm2-7 ring and CDK phosphorylates Sld2, the origin ssDNA binds to CDK-phosphorylated Sld2. This event may allow the interaction between GINS and Mcm2-7 in vivo. Thus, CDK phosphorylation of Sld2 may be important to release Sld2 from Mcm2-7, thereby allowing GINS to bind Mcm2-7. Furthermore, origin ssDNA may stimulate the formation of the CMG complex by alleviating inhibitory interactions between Sld2 with Mcm2-7.
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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.