Gut colonization by Bacteroides requires translation by an EF-G paralog lacking GTPase activity

ABSTRACT: Protein synthesis is crucial for cell growth and survival, yet one of the most energy-consuming cellular processes. How, then, do cells sustain protein synthesis under starvation conditions when energy is limited? To accelerate the translocation of mRNA-tRNAs through the ribosome, bacterial elongation factor G (EF-G) hydrolyzes energy-rich guanosine triphosphate (GTP) for every amino acid incorporated into a protein. Here, we identify an EF-G paralog - EF-G2 - that supports translocation without hydrolyzing GTP in the gut commensal bacterium Bacteroides thetaiotaomicron. EF-G2's singular ability to sustain protein synthesis, albeit at slow rates, is crucial for bacterial gut colonization. EF-G2 is ~10-fold more abundant than canonical EF-G1 in bacteria harvested from murine ceca and,

SUBMITTER: Ms. Weiwei Han 

PROVIDER: S-SCDT-10_15252-EMBJ_2022112372 | biostudies-other |

REPOSITORIES: biostudies-other