A new member of the MCM protein family encoded by the human MCM8 gene, located contrapodal to GCD10 at chromosome band 20p12.3-13

Johnson, Edward M.; Kinoshita, Yayoi; Daniel, Dianne C.

doi:10.1093/nar/gkg395

Cited by 59 publications

(41 citation statements)

References 34 publications

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“…Locations of the primers are specified by distances from the HindIII site at 2325 nt upstream of exon I specified by P1 promoter. myc5F 198, 5Ј-AAGCTGAATTGTGCAGTGCATC-3Ј (528 -549, 22- PCRs were performed as previously described (37). Reactions were carried out with 0.2 mM of each dNTP, 0.3 M primer/each, 10ϫ PCR buffer with Mg 2ϩ , and 1.75 unit of Enzyme mix of the High Fidelity PCR System (Roche Applied Science).…”

Section: Methodsmentioning

confidence: 99%

“…Anti-Cdc6 (Ab-3 mouse monoclonal) was obtained from Oncogene. Immunoprecipitation of MCM proteins from HeLa cell lysates was performed as described previously (37).…”

Section: Methodsmentioning

confidence: 99%

“…There is evidence that MCM7 plays a role in autoregulation of its own gene expression (28). A new member of the MCM protein family has now been discovered, MCM8, which exists exclusively in metazoan organisms (37,48). MCM8 evidently plays a protective role against development of neoplasia (37).…”

Section: Timing Of Dissemination Of Mcm7 Throughout the C-myc Locus Imentioning

confidence: 99%

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Site-specific Loading of an MCM Protein Complex in a DNA Replication Initiation Zone Upstream of the c-MYC Gene in the HeLa Cell Cycle

Kinoshita¹,

Johnson

2004

Journal of Biological Chemistry

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The MCM proteins participate in an orderly association, beginning with the origin recognition complex, that culminates in the initiation of chromosomal DNA replication. Among these, MCM proteins 4, 6, and 7 constitute a subcomplex that reportedly possesses DNA helicase activity. Little is known about DNA sequences initially bound by these MCM proteins or about their cell cycle distribution in the chromatin. We have determined the locations of certain MCM and associated proteins by chromatin immunoprecipitation (ChIP) in a zone of initiation of DNA replication upstream of the c-MYC gene in the HeLa cell cycle. MCM7 and its clamploading partner Cdc6 are highly specifically colocalized by ChIP and re-ChIP in G 1 and early S on a 198-bp segment located near the center of the initiation zone. ChIP and Re-ChIP colocalizes MCM7 and ORC1 to the same segment specifically in late G 1 . MCM proteins 6 and 7 can be coimmunoprecipitated throughout the cell cycle, whereas MCM4 is reduced in the complex in late S and G 2 , reappearing upon mitosis. MCM7 is not visualized by immunohistochemistry on metaphase chromosomes. MCM7 is recruited to multiple sites in chromatin in S and G 2 , at which time it is not detected with ORC1. The rate of dissemination is surprisingly slow and is unlikely to be simply attributed to progression with replication forks. Results indicate sequence-specific loading of MCM proteins onto DNA in late G 1 followed by a recruitment to multiple sites in chromatin subsequent to replication. Members of the minichromosome maintenance (MCM)1 protein family were first characterized in Saccharomyces cerevisiae as essential for plasmid maintenance during the cell cycle (reviewed in Refs. 1-3). Each of the six proteins MCM2, MCM3, MCM4, MCM5, MCM6, and MCM7 has a counterpart in yeast, and each is highly conserved throughout eukaryotes. Deletion of genes encoding any one of these six are lethal in S. cerevisiae or Schizosaccharomyces pombe (3, 4), and these proteins have been ascribed as essential for initiation of DNA replication (5, 6). These proteins have been co-isolated as a single complex, and complexes of various combinations of these proteins have been implicated in licensing DNA for initiation of replication in Xenopus egg extracts (7,8). Another MCM protein, MCM10, is reportedly required for phosphorylation of components of the MCM2-7 complex prior to initiation (9) and has also been implicated in the transition from initiation to replication (10). Preceding initiation of replication, and at a point near the end of mitosis (11), assembly of the MCM proteins into a prereplication complex (pre-RC) occurs dependent on coordinated function of the origin recognition complex (ORC) (12) and proteins Cdc6 (5) and Cdt1 (13). Initiation then depends upon activation by cyclin-dependent kinases (14) and the Dbf4-dependent kinase Cdc7 (15). Evidence derived from temperaturesensitive MCM protein degradation during S-phase (16) and from measurements of MCM protein distribution in chromatin (5) suggests that in S. cerevi...

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Section: Methodsmentioning

confidence: 99%

“…Anti-Cdc6 (Ab-3 mouse monoclonal) was obtained from Oncogene. Immunoprecipitation of MCM proteins from HeLa cell lysates was performed as described previously (37).…”

Section: Methodsmentioning

confidence: 99%

Section: Timing Of Dissemination Of Mcm7 Throughout the C-myc Locus Imentioning

confidence: 99%

See 1 more Smart Citation

Site-specific Loading of an MCM Protein Complex in a DNA Replication Initiation Zone Upstream of the c-MYC Gene in the HeLa Cell Cycle

Kinoshita¹,

Johnson

2004

Journal of Biological Chemistry

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“…84 The MCM8 has been identified in humans and it contains the consensus IDEFDKM and arginine finger motifs. 85,86 The occurrence of GKS motif in Walker A sequence is unique to MCM8. In addition to proliferating cells, filaments.…”

Section: ©2 0 1 1 L a N D E S B I O S C I E N C E D O N O T D I S Tmentioning

confidence: 99%

“…85,86 Recombinant MCM8 displays both DNA helicase and ATPase activities in vitro. 87 The results also indicated involvement of human MCM8 in G 1 phase progression.…”

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confidence: 99%

Genome-wide comprehensive analysis of human helicases

Umate¹,

Tuteja²,

Tuteja³

2011

Communicative & Integrative Biology

105

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Colocalization of MCM8 and MCM7 with proteins involved in distinct aspects of DNA replication

Kinoshita

Johnson

Gordon

et al. 2007

Microscopy Res & Technique

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Minichromosome maintenance (MCM) proteins are essential for DNA replication in eukaryotes. A subcomplex of the MCM2-7 family members, initially characterized in yeast, is thought to serve as a eukaryotic DNA replicative helicase. MCM8 is a new family member, not present in yeast, which may function alone or with other family members in aspects of DNA metabolism, including replication initiation and elongation. Through the use of chromatin immunoprecipitation, we find that MCM8, like MCM7, colocalizes on a specific DNA segment of the c-MYC replication initiation zone (c-MYC replicator) with Cdc6, a protein potentially involved in loading MCM proteins onto DNA. The association between MCM8 and MCM7 peaks in mid G1, at the time of assembly of the prereplication complex. The association of both MCM proteins with Cdc6, however, continues even after DNA replication is complete. We also find that MCM8 colocalizes at the c-MYC replicator with chromatin-bound Cdk2. Our data indicate that any role MCM8 may play in elongation is likely to be discontinuous, in its association with DNA, from a potential role in initiation. Using immunogold electron microscopy we show that MCM8 and MCM7 differ in spatial relation to RPA70 during S phase. Our data strongly suggest that MCM8 functions with other known replication proteins in processes which accompany DNA replication, especially initiation, and which are specifically adapted to suit higher eukaryotes.

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A new member of the MCM protein family encoded by the human MCM8 gene, located contrapodal to GCD10 at chromosome band 20p12.3-13

Cited by 59 publications

References 34 publications

Site-specific Loading of an MCM Protein Complex in a DNA Replication Initiation Zone Upstream of the c-MYC Gene in the HeLa Cell Cycle

Site-specific Loading of an MCM Protein Complex in a DNA Replication Initiation Zone Upstream of the c-MYC Gene in the HeLa Cell Cycle

Genome-wide comprehensive analysis of human helicases

Colocalization of MCM8 and MCM7 with proteins involved in distinct aspects of DNA replication

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