Transposons to toxins: the provenance, architecture and diversification of a widespread class of eukaryotic effectors.

ABSTRACT: Enzymatic effectors targeting nucleic acids, proteins and other cellular components are the mainstay of conflicts across life forms. Using comparative genomics we identify a large class of eukaryotic proteins, which include effectors from oomycetes, fungi and other parasites. The majority of these proteins have a characteristic domain architecture with one of several N-terminal 'Header' domains, which are predicted to play a role in trafficking of these effectors, including a novel version of the Ubiquitin fold. The Headers are followed by one or more diverse C-terminal domains, such as restriction endonuclease (REase), protein kinase, HNH endonuclease, LK-nuclease (a RNase) and multiple distinct peptidase domains, which are predicted to carry their toxicity determinants. The most common t

SUBMITTER: Zhang D 

PROVIDER: S-EPMC4857004 | biostudies-literature | 2016 May

REPOSITORIES: biostudies-literature