Results 51 to 60 of about 11,749,169 (183)

Mcm2 promotes stem cell differentiation via its ability to bind H3-H4

eLife, 2022
Mcm2, a subunit of the minichromosome maintenance proteins 2–7 (Mcm2-7) helicase best known for its role in DNA replication, contains a histone binding motif that facilitates the transfer of parental histones following DNA replication. Here, we show that
Xiaowei Xu, Xu Hua, Kyle Brown, Xiaojun Ren, Zhiguo Zhang   +4 more
doaj   +1 more source

In the absence of ATPase activity, pre-RC formation is blocked prior to MCM2–7 hexamer dimerization [PDF]

, 2013
26.03.14 KB.
Brill, S, Lurz, R, Herrera, MC, Fernández-Cid, A, Speck, C, Clarke, P, Evrin, C, Zech, J, Riera, A   +8 more
core   +2 more sources

Selective role of the DNA helicase Mcm5 in BMP retrograde signaling during Drosophila neuronal differentiation.

PLoS Genetics, 2022
The MCM2-7 complex is a highly conserved hetero-hexameric protein complex, critical for DNA unwinding at the replicative fork during DNA replication. Overexpression or mutation in MCM2-7 genes is linked to and may drive several cancer types in humans. In
Irene Rubio-Ferrera, Pablo Baladrón-de-Juan, Luis Clarembaux-Badell, Marta Truchado-Garcia, Sheila Jordán-Álvarez, Stefan Thor, Jonathan Benito-Sipos, Ignacio Monedero Cobeta   +7 more
doaj   +1 more source

Stepwise Regulated Chromatin Assembly of MCM2–7 Proteins [PDF]

Journal of Biological Chemistry, 2000
Acquisition of the competence to replicate requires the assembly of the MCM2-7 (minichromosome maintenance) protein complex onto pre-replicative chromatin, a step of the licensing reaction. This step is thought to occur through binding of a heterohexameric MCM complex containing the six related MCM subunits.
D, Maiorano, J M, Lemaître, M, Méchali
openaire   +2 more sources

The Mcm2-7 Complex Has In Vitro Helicase Activity [PDF]

Molecular Cell, 2008
Helicases unwind duplex DNA ahead of the polymerases at the replication fork. However, the identity of the eukaryotic replicative helicase has been controversial; in vivo studies implicate the ring-shaped heterohexameric Mcm2-7 complex, although only a specific subset of Mcm subunits (Mcm467) unwind DNA in vitro.
Bochman, Matthew L., Schwacha, Anthony
openaire   +2 more sources

Validation of a high throughput screening assay to identify small molecules that target the eukaryotic replicative helicase

SLAS Discovery, 2022
Mcm2-7 is the catalytic core of the eukaryotic replicative helicase, which together with CDC45 and the GINS complex unwind parental DNA to generate templates for DNA polymerase.
Jordan Sanders, Michael Castiglione, Tongying Shun, Laura L. Vollmer, Mark E. Schurdak, Andreas Vogt, Anthony Schwacha   +6 more
doaj   +1 more source

Mcm2-, Mcm4-, and Mcm6-ChEC footprints over 12 origins on chrIV.

, 2021
Footprints for Mcm2-ChEC (top row), Mcm4-ChEC (second row), and Mcm6-ChEC (third row) resemble each other at each of 12 consecutive origins on chrIV, but free MNase (bottom row) does not.
Tonibelle Gatbonton-Schwager (5707766), Hyunchang Kwak (7538330), Uyen Lao (422297), Antonio Bedalov (15251), Eric J. Foss (206758), Adam H. Thiesen (6694139), Smitha Sripathy (5707769)   +6 more
core   +1 more source

Activation of the MCM2-7 Helicase by Association with Cdc45 and GINS Proteins [PDF]

Molecular Cell, 2010
MCM2-7 proteins provide essential helicase functions in eukaryotes at chromosomal DNA replication forks. During the G1 phase of the cell cycle, they remain loaded on DNA but are inactive. We have used recombinant methods to show that the Drosophila MCM2-7 helicase is activated in complex with Cdc45 and the four GINS proteins (CMG complex).
Ilves, Ivar, Petojevic, Tatjana, Pesavento, James J., Botchan, Michael R.   +3 more
openaire   +2 more sources

Cryo-EM structure of a helicase loading intermediate containing ORC-Cdc6-Cdt1-MCM2-7 bound to DNA [PDF]

, 2013
26.03.14 KB.
Cecile Evrin, Kawakami, H, Li, H, Riera, A, Alejandra Fernández-Cid, Jingchuan Sun, Riera, A., Stillman, B, Stillman, B., Stefan A Samel, Christian Speck, Hironori Kawakami, Speck, C., Samel, S. A., Fernandez-Cid, A., Samel, AS, Speck, C, Sun, J., Sun, J, Fernandez-Cid, A, Huilin Li, Evrin, C., Kawakami, H., Evrin, C, Li, H., Alberto Riera, Bruce Stillman   +26 more
core   +1 more source

Structural mechanism for replication origin binding and remodeling by a metazoan origin recognition complex and its co-loader Cdc6

Nature Communications, 2020
The origin recognition complex (ORC) is essential for loading the Mcm2–7 replicative helicase onto DNA during DNA replication initiation. Here, the authors describe several cryo-electron microscopy structures of Drosophila ORC bound to DNA and its ...
Jan Marten Schmidt, Franziska Bleichert
doaj   +1 more source