Archaeal β-CASP ribonucleases of the aCPSF1 family are orthologs of the eukaryal CPSF-73 factor.

ABSTRACT: Bacterial RNase J and eukaryal cleavage and polyadenylation specificity factor (CPSF-73) are members of the β-CASP family of ribonucleases involved in mRNA processing and degradation. Here we report an in-depth phylogenomic analysis that delineates aRNase J and archaeal CPSF (aCPSF) as distinct orthologous groups and establishes their repartition in 110 archaeal genomes. The aCPSF1 subgroup, which has been inherited vertically and is strictly conserved, is characterized by an N-terminal extension with two K homology (KH) domains and a C-terminal motif involved in dimerization of the holoenzyme. Pab-aCPSF1 (Pyrococcus abyssi homolog) has an endoribonucleolytic activity that preferentially cleaves at single-stranded CA dinucleotides and a 5'-3' exoribonucleolytic activity that acts on 5' mon

SUBMITTER: Phung DK 

PROVIDER: S-EPMC3553952 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature