Biochemical analysis of components of the pre-replication complex of Archaeoglobus fulgidus

Grainge, Ian; Scaife, Sarah; Wigley, Dale B.

doi:10.1093/nar/gkg662

Cited by 61 publications

(74 citation statements)

References 29 publications

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“…However, in contrast with our results, the A. fulgidus Cdc6 factor was found to displace MCM hexamers bound to these DNA molecules (21). It is interesting to note that in a recent sequence analysis of the Cdc6-like proteins from various archaeal species, SsoCdc6-2 and the above A. fulgidus Cdc6 factor were reported to belong to different phylogenetic clades, thus being likely that they may play different roles at the replication origins (22).…”

Section: Figcontrasting

confidence: 99%

A CDC6-like Factor from the Archaea Sulfolobus solfataricus Promotes Binding of the Mini-chromosome Maintenance Complex to DNA

Felice

Esposito²,

Pucci³

et al. 2004

Journal of Biological Chemistry

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The archaeal replication apparatus appears to be a simplified version of the eukaryotic one with fewer polypeptides and simpler protein complexes. Herein, we report evidence that a Cdc6-like factor from the hyperthermophilic crenarchaea Sulfolobus solfataricus stimulates binding of the homohexameric MCM-like complex to bubble-and fork-containing DNA oligonucleotides that mimic early replication intermediates. This function does not require the Cdc6 ATP and DNA binding activities. These findings may provide important clues to understanding how the DNA replication initiation process has evolved in the more complex eukaryotic organisms.Living organisms have evolved different strategies to recruit and load DNA helicases at the replication origins, and accessory factors, referred to as helicase loaders, are required to accomplish this task (1, 2). The helicase loading process was best characterized at the molecular level in two bacterial systems: Escherichia coli (3) and Bacillus subtilis (4). The E. coli replicative homohexameric DNA helicase DnaB associates with its loader, DnaC, forming a 6:6 complex that is recruited at the chromosomal replication origin (oriC) by the initiator protein DnaA (5). DnaB is then released in an active form, and this initiates formation of two replication forks that extend in opposite directions from oriC (6). Because E. coli DnaB forms stable hexamers in solution that are unable to efficiently selfload onto single-stranded DNA, it was proposed that its loading by DnaC is carried out by a ring-breaking mechanism (1). A similar ring-opening/closing mechanism was demonstrated to take place during loading of the E. coli phage T7 gp4 DNA helicase/primase, but in this case no accessory loading factor is required (7). In B. subtilis, the replicative DNA helicase DnaC forms homohexamers in solution in the presence of ATP, but without ATP the hexameric form readily dissociates into monomers. The preformed hexameric DnaC helicase is unable to unwind DNA and instead must be assembled from monomers around DNA by a loading system that consists of two proteins, DnaI and DnaB (4). A ring-forming mechanism was also proposed for the E. coli bacteriophage T4 helicase gp41 (8) and for the simian virus 40 large tumor antigen, but in this latter case a separate helicase loader is not required (1, 9).

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Section: Figcontrasting

confidence: 99%

A CDC6-like Factor from the Archaea Sulfolobus solfataricus Promotes Binding of the Mini-chromosome Maintenance Complex to DNA

Felice

Esposito²,

Pucci³

et al. 2004

Journal of Biological Chemistry

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“…Although all proteins are homologous, they appear to aggregate differently. Although the mtMCM appears to form double hexamers (10 -13), the enzymes from S. solfataricus (16), A. fulgidus, and Aeropyrum pernix (18) are hexamers. Electron micrograph reconstruction of mtMCM revealed ring-shaped hexamers (20) or heptamers (21), but no dodecamers could be observed.…”

Section: Discussionmentioning

confidence: 99%

“…Biochemical studies with the MCM proteins of Methanothermobacter thermautotrophicus (mt) (10 -15), Sulfolobus solfataricus (16,17), and Archaeoglobus fulgidus (18) revealed that the enzymes possess biochemical properties similar to those of the eukaryotic Mcm4,6,7 complex: 3Ј 3 5Ј helicase, ssDNA binding, and DNA-dependent ATPase activity plus double-stranded (ds) DNA translocation.…”

mentioning

confidence: 99%

“…The MCM homologues of S. solfataricus (16) and A. fulgidus (18) form hexamers in solution, but mtMCM appears to form dodecamers (10 -13). The crystal structure of the N-terminal portion of the mtMCM protein suggested a dodecameric structure (19).…”

mentioning

confidence: 99%

“…However, biochemical analysis of a zinc finger mutant showed that the mutant protein is impaired in ssDNA binding but not double hexamer formation (13). In addition, studies with the A. fulgidus MCM suggested that domain B, which contains the zinc finger, is not needed for multimerization (18) but probably for ssDNA binding.…”

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confidence: 99%

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Biochemical Characterization of the Methanothermobacter thermautotrophicus Minichromosome Maintenance (MCM) Helicase N-terminal Domains

Kasiviswanathan

Shin

Melamud

et al. 2004

Journal of Biological Chemistry

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Minichromosome maintenance helicases are ringshaped complexes that play an essential role in archaeal and eukaryal DNA replication by separating the two strands of chromosomal DNA to provide the singlestranded substrate for the replicative polymerases. For the archaeal protein it was shown that the N-terminal portion of the protein, which is composed of domains A, B, and C, is involved in multimer formation and singlestranded DNA binding and may also play a role in regulating the helicase activity. Here, a detailed biochemical characterization of the N-terminal region of the Methanothermobacter thermautotrophicus minichromosome maintenance helicase is described. Using biochemical and biophysical analyses it is shown that domain C of the N-terminal portion, located adjacent to the helicase catalytic domains, is required for protein multimerization and that domain B is the main contact region with single-stranded DNA. It is also shown that although oligomerization is not essential for single-stranded DNA binding and ATPase activity, the presence of domain C is essential for helicase activity.

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Biochemical analysis of components of the pre-replication complex of Archaeoglobus fulgidus

Cited by 61 publications

References 29 publications

A CDC6-like Factor from the Archaea Sulfolobus solfataricus Promotes Binding of the Mini-chromosome Maintenance Complex to DNA

A CDC6-like Factor from the Archaea Sulfolobus solfataricus Promotes Binding of the Mini-chromosome Maintenance Complex to DNA

Biochemical Characterization of the Methanothermobacter thermautotrophicus Minichromosome Maintenance (MCM) Helicase N-terminal Domains

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