Bacterial mode of replication with eukaryotic-like machinery in a hyperthermophilic archaeon

Science. 2000 Jun 23;288(5474):2212-5. doi: 10.1126/science.288.5474.2212.

Abstract

Despite a rapid increase in the amount of available archaeal sequence information, little is known about the duplication of genetic material in the third domain of life. We identified a single origin of bidirectional replication in Pyrococcus abyssi by means of in silico analyses of cumulative oligomer skew and the identification of an early replicating chromosomal segment. The replication origin in three Pyrococcus species was found to be highly conserved, and several eukaryotic-like DNA replication genes were clustered around it. As in Bacteria, the chromosomal region containing the replication terminus was a hot spot of genome shuffling. Thus, although bacterial and archaeal replication proteins differ profoundly, they are used to replicate chromosomes in a similar manner in both prokaryotic domains.

Publication types

  • Comment
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Archaeal Proteins / genetics
  • Archaeal Proteins / metabolism
  • Bacteria / genetics
  • Bacteria / metabolism
  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / metabolism
  • Chromosomes, Archaeal / metabolism*
  • Conserved Sequence
  • DNA Helicases / genetics
  • DNA Helicases / metabolism
  • DNA Replication / genetics*
  • DNA, Archaeal / biosynthesis*
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism
  • Eukaryotic Cells / metabolism
  • Evolution, Molecular
  • Genes, Archaeal
  • Genome, Archaeal*
  • Origin Recognition Complex
  • Puromycin / pharmacology
  • Pyrococcus / genetics*
  • Pyrococcus / metabolism*
  • Replication Origin
  • Saccharomyces cerevisiae Proteins*

Substances

  • Archaeal Proteins
  • CDC6 protein, S cerevisiae
  • Cell Cycle Proteins
  • DNA, Archaeal
  • DNA-Binding Proteins
  • Origin Recognition Complex
  • Saccharomyces cerevisiae Proteins
  • Puromycin
  • DNA Helicases
  • MCM protein, Methanobacterium thermoautotrophicum