scholarly journals Polymorphism and Double Hexamer Structure in the Archaeal Minichromosome Maintenance (MCM) Helicase fromMethanobacterium thermoautotrophicum

2005 ◽  
Vol 280 (49) ◽  
pp. 40909-40915 ◽  
Author(s):  
Yacob Gómez-Llorente ◽  
Ryan J. Fletcher ◽  
Xiaojiang S. Chen ◽  
José M. Carazo ◽  
Carmen San Martín
Keyword(s):  
Minichromosome Maintenance ◽  
Mcm Helicase

scholarly journals DNA Binding by the Methanothermobacter thermautotrophicus Cdc6 Protein Is Inhibited by the Minichromosome Maintenance Helicase

2006 ◽  
Vol 188 (12) ◽  
pp. 4577-4580 ◽  
Author(s):  
Rajesh Kasiviswanathan ◽  
Jae-Ho Shin ◽  
Zvi Kelman
Keyword(s):  
Dna Binding ◽  
Binding Activity ◽  
Minichromosome Maintenance ◽  
Single Stranded Dna ◽  
Mutant Proteins ◽  
Dna Binding Activity ◽  
Double Stranded Dna ◽  
Mcm Helicase ◽  
Methanothermobacter Thermautotrophicus

ABSTRACT The Cdc6 proteins from the archaeon Methanothermobacter thermautotrophicus were previously shown to bind double-stranded DNA. It is shown here that the proteins also bind single-stranded DNA. Using minichromosome maintenance (MCM) helicase mutant proteins unable to bind DNA, it was found that the interaction of MCM with Cdc6 inhibits the DNA binding activity of Cdc6.

scholarly journals The interplay of DNA binding, ATP hydrolysis and helicase activities of the archaeal MCM helicase

2011 ◽  
Vol 436 (2) ◽  
pp. 409-414 ◽  
Author(s):  
Li Phing Liew ◽  
Stephen D. Bell
Keyword(s):  
Dna Binding ◽  
Active Site ◽  
Atp Hydrolysis ◽  
Sulfolobus Solfataricus ◽  
Active Form ◽  
Dna Helicase ◽  
Atpase Domain ◽  
Minichromosome Maintenance ◽  
Conserved Residues ◽  
Mcm Helicase

The MCM (minichromosome maintenance) proteins of archaea are widely believed to be the replicative DNA helicase of these organisms. Most archaea possess a single MCM orthologue that forms homo-multimeric assemblies with a single hexamer believed to be the active form. In the present study we characterize the roles of highly conserved residues in the ATPase domain of the MCM of the hyperthermophilic archaeon Sulfolobus solfataricus. Our results identify a potential conduit for communicating DNA-binding information to the ATPase active site.

The MCM complex: (just) a replicative helicase?

2008 ◽  
Vol 36 (1) ◽  
pp. 136-140 ◽  
Author(s):  
Alessandro Costa ◽  
Silvia Onesti
Keyword(s):  
Minichromosome Maintenance ◽  
Replicative Helicase ◽  
Aaa Atpase ◽  
Mcm Helicase ◽  
Eukaryotic Dna ◽  
Mcm Complex ◽  
Elongation Step ◽  
Hexameric Helicases

The MCM2–MCM7 (minichromosome maintenance 2–7) complex is involved both in the initiation and the elongation step of eukaryotic DNA replication and is believed to be the replicative helicase. Whereas the mechanism of DNA unwinding at the replication fork has been extensively investigated, the role of the MCM2–MCM7 complex during initiation has not yet been characterized by biochemical studies. Here we summarize the in vivo evidence which supports a role for the MCM complex in origin melting. In addition, we present an overview of the mechanism of action of a number of AAA+ (ATPase associated with various cellular activities) initiators and hexameric helicases, which can be used in turn as models for the steps of recognition, duplex melting, loading and nucleic acid translocation of the MCM helicase.

scholarly journals Mutations in Subdomain B of the Minichromosome Maintenance (MCM) Helicase Affect DNA Binding and Modulate Conformational Transitions

2008 ◽  
Vol 284 (9) ◽  
pp. 5654-5661 ◽  
Author(s):  
Elizabeth R. Jenkinson ◽  
Alessandro Costa ◽  
Andrew P. Leech ◽  
Ardan Patwardhan ◽  
Silvia Onesti ◽  
...  
Keyword(s):  
Dna Binding ◽  
Conformational Transitions ◽  
Minichromosome Maintenance ◽  
Mcm Helicase

Structure and function of the GINS complex, a key component of the eukaryotic replisome

2010 ◽  
Vol 425 (3) ◽  
pp. 489-500 ◽  
Author(s):  
Stuart A. MacNeill
Keyword(s):  
Replication Fork ◽  
Biochemical Analysis ◽  
Current Knowledge ◽  
Chromosomal Dna ◽  
Minichromosome Maintenance ◽  
Replication Process ◽  
Replicative Helicase ◽  
Cellular Life ◽  
Mcm Helicase ◽  
And Function

High-fidelity chromosomal DNA replication is fundamental to all forms of cellular life and requires the complex interplay of a wide variety of essential and non-essential protein factors in a spatially and temporally co-ordinated manner. In eukaryotes, the GINS complex (from the Japanese go-ichi-ni-san meaning 5-1-2-3, after the four related subunits of the complex Sld5, Psf1, Psf2 and Psf3) was recently identified as a novel factor essential for both the initiation and elongation stages of the replication process. Biochemical analysis has placed GINS at the heart of the eukaryotic replication apparatus as a component of the CMG [Cdc45–MCM (minichromosome maintenance) helicase–GINS] complex that most likely serves as the replicative helicase, unwinding duplex DNA ahead of the moving replication fork. GINS homologues are found in the archaea and have been shown to interact directly with the MCM helicase and with primase, suggesting a central role for the complex in archaeal chromosome replication also. The present review summarizes current knowledge of the structure, function and evolution of the GINS complex in eukaryotes and archaea, discusses possible functions of the GINS complex and highlights recent results that point to possible regulation of GINS function in response to DNA damage.

scholarly journals The Methanothermobacter thermautotrophicus Cdc6-2 Protein, the Putative Helicase Loader, Dissociates the Minichromosome Maintenance Helicase

2008 ◽  
Vol 190 (11) ◽  
pp. 4091-4094 ◽  
Author(s):  
Jae-Ho Shin ◽  
Gun Young Heo ◽  
Zvi Kelman
Keyword(s):  
Minichromosome Maintenance ◽  
Mcm Helicase ◽  
Protein Functions ◽  
Mcm Complex ◽  
Methanothermobacter Thermautotrophicus

ABSTRACT The Cdc6-1 and -2 proteins from the archaeon Methanothermobacter thermautotrophicus were previously shown to bind the minichromosome maintenance (MCM) helicase. It is shown here that Cdc6-2 protein dissociates the MCM complex. This observation supports the hypothesis that the Cdc6-2 protein functions as a helicase loader.

scholarly journals Rapid DNA replication origin licensing protects stem cell pluripotency

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Jacob Peter Matson ◽  
Raluca Dumitru ◽  
Philip Coryell ◽  
Ryan M Baxley ◽  
Weili Chen ◽  
...  
Keyword(s):  
Stem Cells ◽  
Dna Replication ◽  
Cell Types ◽  
Minichromosome Maintenance ◽  
Origin Licensing ◽  
Mcm Helicase ◽  
Dna Replication Origin ◽  
Stem Cell Pluripotency ◽  
Dna Replication Origins ◽  
Intrinsic Characteristic

Complete and robust human genome duplication requires loading minichromosome maintenance (MCM) helicase complexes at many DNA replication origins, an essential process termed origin licensing. Licensing is restricted to G1 phase of the cell cycle, but G1 length varies widely among cell types. Using quantitative single-cell analyses, we found that pluripotent stem cells with naturally short G1 phases load MCM much faster than their isogenic differentiated counterparts with long G1 phases. During the earliest stages of differentiation toward all lineages, MCM loading slows concurrently with G1 lengthening, revealing developmental control of MCM loading. In contrast, ectopic Cyclin E overproduction uncouples short G1 from fast MCM loading. Rapid licensing in stem cells is caused by accumulation of the MCM loading protein, Cdt1. Prematurely slowing MCM loading in pluripotent cells not only lengthens G1 but also accelerates differentiation. Thus, rapid origin licensing is an intrinsic characteristic of stem cells that contributes to pluripotency maintenance.

scholarly journals Chromatin loading of MCM hexamers is associated with di-/tri-methylation of histone H4K20 toward S phase entry

2021 ◽  
Author(s):  
Yoko Hayashi-Takanaka ◽  
Yuichiro Hayashi ◽  
Yasuhiro Hirano ◽  
Atsuko Miyawaki-Kuwakado ◽  
Yasuyuki Ohkawa ◽  
...  
Keyword(s):  
Dna Replication ◽  
S Phase ◽  
G1 Phase ◽  
Histone H4 ◽  
Replication Origins ◽  
Minichromosome Maintenance ◽  
Limiting Step ◽  
Mcm Helicase ◽  
Dna Replication Origins ◽  
Phase Entry

Replication of genomic DNA is a key step in initiating cell proliferation. Loading hexameric complexes of minichromosome maintenance (MCM) helicase on DNA replication origins during the G1 phase is essential in initiating DNA replication. Here, we show that stepwise loading of two hexamer complexes of MCM occurs during G1 progression in human cells. This transition from the single-to-double hexamer was associated with levels of methylation at lysine 20 of histone H4 (H4K20). A single hexamer of MCM complexes was loaded at the replication origins with the presence of H4K20 monomethylation (H4K20me1) in the early G1 phase, then another single hexamer was recruited to form a double hexamer later in G1 as H4K20me1 was converted to di-/tri-methylation (H4K20me2/me3). Under non-proliferating conditions, cells stay halted at the single-hexamer state in the presence of H4K20me1. We propose that the single-hexamer state on chromatin is a limiting step in making the proliferation-quiescence decision.

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