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Knockdown of both HP1a and Mcm10 genes inhibited the progression of S phase in eye imaginal discs. Proximity Ligation Assay (PLA) demonstrated that HP1a is in close proximity to DNA replication proteins including Mcm10, RFC140 and DNA polymerase epsilon 255 kDa subunit in S-phase.
Observation of embryonic nuclear morphology and quantification of embryo hatch rates reveal that maternal loading of Mcm10 is required for embryonic nuclear stability, and suggest a role for Mcm10 post zygotic transition.
Data show that Mcm10 has a role in heterochromatic silencing and chromosome condensation.
Results show that MCM10 is significantly upregulated in urothelial carcinoma (UC), and associated with tumor aggressiveness. Its knockdown significantly suppressed cell proliferation in UC cell lines.
Data suggest that interaction of Mcm10 with Mcm2-7 multimer requires Mcm10 domain that contains amino acids 530-655, which overlaps with domain required for stable retention of Mcm10 on chromatin; Mcm10 conserved domain (amino acids 200-482) is essential for DNA replication; both conserved domain and Mcm2-7-binding domain are required for full activity of Mcm10.
RecQL4-dependent association of Mcm10 and Ctf4 with replication origins appears to be the first important step controlled by S phase promoting kinases and checkpoint pathways for the initiation of DNA replication in human cells.
MCM10 is the natural substrate of the Cul4-DDB1[VprBP] E3 ubiquitin ligase whose degradation is regulated by VprBP, but Vpr enhances the proteasomal degradation of MCM10 by interacting with VprBP.
Loss of Mcm10 engages checkpoint, DNA repair and SUMO-dependent rescue pathways that collectively counteract replication stress and chromosome breakage. [Review]
Mcm10 utilizes a modular architecture to act as a replisome scaffold, which helps to define possible roles in origin DNA melting, Pol alpha recruitment and coordination of enzymatic activities during elongation.
Data suggest that CDC45 and MCM10 (minichromosome maintenance complex component 10) directly interact and establish a mutual co-operation in DNA binding; key domains appear to interact and then interact with DNA inside cells or in cell-free systems.
This report shows that human Mcm10 is an acetylated protein regulated by SIRT1, which binds and deacetylates Mcm10 both in vivo and in vitro, and modulates Mcm10 stability and ability to bind DNA.
High doses of ionizing gamma radiation and exposure to a combination of DNA-damaging chemicals do not decrease Mcm10 protein levels, demonstrating that Mcm10 down-regulation is triggered only by UV-specific damage
human Mcm10 is temporarily recruited to the replication sites 30-60 min before they replicate and dissociates from chromatin after the activation of the prereplication complex
transcription of human MCM10 and TopBP1 is activated by transcription factors E2F1-3, but not by factors E2F4-7
These results argue that cells can tolerate low levels of p180 as long as Mcm10 is present to "recycle" it.
Mcm10 is required for chromatin loading of And-1.
Results show that MCM10 molecule is a ring-shaped hexamer with large central and smaller lateral channels and a system of inner chambers.
MCM10 is essential for the efficient elongation step of chromosome replication.
These results indicate that MCM10 protein is essential for maintaining genome integrity as well as cell cycle progression.
DNA and p180 binding to an Mcm10 construct that contains both the ID and CTD, provide the first mechanistic insight into how Mcm10 might use a handoff mechanism to load and stabilize pol alpha within the replication fork.
MCM10 interacts directly with RECQ4 and regulates its DNA unwinding activity.
Assembly of the Cdc45-Mcm2-7-GINS complex requires the Ctf4/And-1, RecQL4, and Mcm10 proteins.
Functional studies of the Drosophila homolog
the absence of Mcm10 or its phosphorylation by CDK results in instability of replisome proteins on DNA, which is particularly important under conditions of replication stress.
Dna2 co-localizes in foci with RPA and is found in a complex with replication fork components And-1 and Mcm10. Dna2 interacts with the DSB repair and checkpoint proteins Nbs1 and ATM.
insight in the action of Mcm10 in the replisome
analysis of domain architecture and biochemical characterization of vertebrate Mcm10
Structural basis for DNA binding by replication initiator Mcm10 is reported.
The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are involved in the initiation of eukaryotic genome replication. The hexameric protein complex formed by MCM proteins is a key component of the pre-replication complex (pre-RC) and it may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins. This protein can interact with MCM2 and MCM6, as well as with the origin recognition protein ORC2. It is regulated by proteolysis and phosphorylation in a cell cycle-dependent manner. Studies of a similar protein in Xenopus suggest that the chromatin binding of this protein at the onset of DNA replication is after pre-RC assembly and before origin unwinding. Alternatively spliced transcript variants encoding distinct isoforms have been identified.
, sensitized chromosome inheritance modifier 19
, MCM10 minichromosome maintenance deficient 10
, homolog of yeast MCM10
, protein MCM10 homolog
, minichromosome maintenance deficient 10