Crystal structure of an archaeal cleavage and polyadenylation specificity factor subunit from Pyrococcus horikoshii.

摘要

In eukaryotes, cleavage and polyadenylation specificity factor (CPSF) is an important multisubunit complex required for 3'-end cleavage of the transcript as well as for subsequent polyadenylation during the maturation of the 3'-end of mRNA. In this family of protein factors, CPSF-73 and CPSF-100 are members of the metallo-beta-lactamase superfamily and CPSF-73 is a ribonuclease involved in maturation of the 3'-end of mRNA. beta-CASP family proteins are widely distributed in eukaryotes, bacteria, and archaea and belong to a group of novel nuclease proteins in the metallo-beta-lactamase super-family. beta-CASP family proteins are named after the metallo-beta-lactamase-associated CPSF Artemis SNM1/ PSO2, and they commonly comprise a metallo-beta-lactamase domain and a beta-CASP domain, with the active site located between these two domains.