Ribonucleotide reductase in the archaeon Pyrococcus furiosus: a critical enzyme in the evolution of DNA genomes?

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TitleRibonucleotide reductase in the archaeon Pyrococcus furiosus: a critical enzyme in the evolution of DNA genomes?
Publication TypeJournal Article
Year of Publication1997
AuthorsRiera, J, Robb, FT, Weiss, R, Fontecave, M
JournalProc Natl Acad Sci U S A
Volume94
Issue2
Pagination475-8
Date Published1997 Jan 21
ISSN0027-8424
KeywordsAmino Acid Sequence, Archaea, Biological Evolution, Cysteine, DNA, Genes, Bacterial, Molecular Sequence Data, Ribonucleotide Reductases, RNA, Sequence Alignment, Sequence Homology, Amino Acid
Abstract

Ribonucleotide reductase (RNR), the enzyme responsible for deoxyribonucleotide synthesis, has been isolated from Pyrococcus furiosus, a deeply branching hyperthermophilic, strictly anaerobic archaeon. Its gene has been cloned, sequenced, and shown to harbor two insertions encoding inteins. The purified enzyme absolutely requires adenosylcobalamin for activity, a trait that defines it as a member of class II (adenosyl-cobalamin-dependent) prokaryotic RNRs. On the other hand, the archaeal RNR has significant amino acid sequence homology with class I (aerobic non-heme iron-dependent) and class III (anaerobic iron-sulfur-dependent) RNRs present in eukaryotes and bacteria, respectively. It is proposed that this enzyme may be the closest possible relative of the original RNR, which allowed the key "RNA world" to "DNA world" transition, and that the different classes of present-day RNRs are the products of divergent evolution.

Alternate JournalProc. Natl. Acad. Sci. U.S.A.
PubMed ID9012808
PubMed Central IDPMC19537