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ABC‐F translation factors: from antibiotic resistance to immune response
Author(s) -
Fostier Corentin R.,
Monlezun Laura,
Ousalem Farès,
Singh Shikha,
Hunt John F.,
Boël Grégory
Publication year - 2021
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13984
Subject(s) - peptidyl transferase , ribosome , translation (biology) , biology , transfer rna , protein biosynthesis , genetics , ribosomal rna , ribosomal protein , function (biology) , microbiology and biotechnology , elongation factor , computational biology , gene , rna , messenger rna
Energy‐dependent translational throttle A (EttA) from Escherichia coli is a paradigmatic ABC‐F protein that controls the first step in polypeptide elongation on the ribosome according to the cellular energy status. Biochemical and structural studies have established that ABC‐F proteins generally function as translation factors that modulate the conformation of the peptidyl transferase center upon binding to the ribosomal tRNA exit site. These factors, present in both prokaryotes and eukaryotes but not in archaea, use related molecular mechanisms to modulate protein synthesis for heterogenous purposes, ranging from antibiotic resistance and rescue of stalled ribosomes to modulation of the mammalian immune response. Here, we review the canonical studies characterizing the phylogeny, regulation, ribosome interactions, and mechanisms of action of the bacterial ABC‐F proteins, and discuss the implications of these studies for the molecular function of eukaryotic ABC‐F proteins, including the three human family members.