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

Autor: Han W; Department of Microbial Pathogenesis, Yale School of Medicine, New Haven, CT, USA.; Yale Microbial Sciences Institute, West Haven, CT, USA., Peng BZ; Department of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany., Wang C; Department of Microbial Pathogenesis, Yale School of Medicine, New Haven, CT, USA.; Yale Microbial Sciences Institute, West Haven, CT, USA., Townsend GE 2nd; Department of Microbial Pathogenesis, Yale School of Medicine, New Haven, CT, USA.; Yale Microbial Sciences Institute, West Haven, CT, USA., Barry NA; Department of Microbial Pathogenesis, Yale School of Medicine, New Haven, CT, USA.; Yale Microbial Sciences Institute, West Haven, CT, USA., Peske F; Department of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany., Goodman AL; Department of Microbial Pathogenesis, Yale School of Medicine, New Haven, CT, USA.; Yale Microbial Sciences Institute, West Haven, CT, USA., Liu J; Department of Microbial Pathogenesis, Yale School of Medicine, New Haven, CT, USA.; Yale Microbial Sciences Institute, West Haven, CT, USA., Rodnina MV; Department of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany., Groisman EA; Department of Microbial Pathogenesis, Yale School of Medicine, New Haven, CT, USA.; Yale Microbial Sciences Institute, West Haven, CT, USA.
Jazyk: angličtina
Zdroj: The EMBO journal [EMBO J] 2023 Jan 16; Vol. 42 (2), pp. e112372. Date of Electronic Publication: 2022 Dec 06.
DOI: 10.15252/embj.2022112372
Abstrakt: 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, unlike EF-G1, specifically accumulates during carbon starvation. Moreover, we uncover a 26-residue region unique to EF-G2 that is essential for protein synthesis, EF-G2 dissociation from the ribosome, and responsible for the absence of GTPase activity. Our findings reveal how cells curb energy consumption while maintaining protein synthesis to advance fitness in nutrient-fluctuating environments.
(© 2022 The Authors.)
Databáze: MEDLINE
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