Extended C-terminus and length of the linker connecting the G-domains are species-specific variations in the EngA family of GTPases

EngA is an essential protein involved in ribosome biogenesis. It is an unique GTPase, possessing two consecutive G-domains. Using sequence and phylogenetic analysis, we found two intriguing variants among EngA homologues – one with a shorter linker joining the G-domains and another with a longer linker, which additionally possesses an extended C-terminus. Interestingly, while the former variant is mainly restricted to firmicutes, the latter is found in nonfirmicutes. Chimeric proteins with interchanged linkers and extensions were generated to gauge the importance of these elements. Ribosome interaction experiments employing the chimeric proteins suggest that a precise combination of the linker and C-terminal extension are important features regulating EngA ribosome interactions in a variant-specific manner.

▸ Homologues of the GTPase EngA exist as two distinct variants. ▸ EngA from firmicutes have smaller linkers connecting the G-domains. ▸ A longer linker and an extended C-terminus are found in nonfirmicute homologues. ▸ These species-specific features appear to regulate the EngA–ribosome association.