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Biol Direct. 2015 Oct 29;10:65. doi: 10.1186/s13062-015-0093-2.

Evolution of an archaeal virus nucleocapsid protein from the CRISPR-associated Cas4 nuclease.

Author information

1
Department of Microbiology, Unité Biologie Moléculaire du Gène chez les Extrêmophiles, Institut Pasteur, Paris, 75015, France. krupovic@pasteur.fr.
2
Department of Microbiology, Unité Biologie Moléculaire du Gène chez les Extrêmophiles, Institut Pasteur, Paris, 75015, France. virginija.cvirkaite-krupovic@pasteur.fr.
3
Department of Microbiology, Unité Biologie Moléculaire du Gène chez les Extrêmophiles, Institut Pasteur, Paris, 75015, France. david.prangishvili@pasteur.fr.
4
National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD, 20894, USA. koonin@ncbi.nlm.nih.gov.

Abstract

Many proteins of viruses infecting hyperthermophilic Crenarchaeota have no detectable homologs in current databases, hampering our understanding of viral evolution. We used sensitive database search methods and structural modeling to show that a nucleocapsid protein (TP1) of Thermoproteus tenax virus 1 (TTV1) is a derivative of the Cas4 nuclease, a component of the CRISPR-Cas adaptive immunity system that is encoded also by several archaeal viruses. In TTV1, the Cas4 gene was split into two, with the N-terminal portion becoming TP1, and lost some of the catalytic amino acid residues, apparently resulting in the inactivation of the nuclease. To our knowledge, this is the first described case of exaptation of an enzyme for a virus capsid protein function.

PMID:
26514828
PMCID:
PMC4625639
DOI:
10.1186/s13062-015-0093-2
[Indexed for MEDLINE]
Free PMC Article

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