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- Title
Stall no more at polyproline stretches with the translation elongation factors EF-P and IF-5A.
- Authors
Lassak, Jürgen; Wilson, Daniel N.; Jung, Kirsten
- Abstract
Synthesis of polyproline proteins leads to translation arrest. To overcome this ribosome stalling effect, bacteria depend on a specialized translation elongation factor P ( EF-P), being orthologous and functionally identical to eukaryotic/archaeal elongation factor e/a IF-5 A (recently renamed ' EF5'). EF- P binds to the stalled ribosome between the peptidyl-t RNA binding and t RNA-exiting sites, and stimulates peptidyl-transferase activity, thus allowing translation to resume. In their active form, both EF- P and e/a IF-5 A are post-translationally modified at a positively charged residue, which protrudes toward the peptidyl-transferase center when bound to the ribosome. While archaeal and eukaryotic IF-5 A strictly depend on (deoxy-) hypusination (hypusinylation) of a conserved lysine, bacteria have evolved diverse analogous modification strategies to activate EF- P. In E scherichia coli and S almonella enterica a lysine is extended by β-lysinylation and subsequently hydroxylated, whereas in P seudomonas aeruginosa and S hewanella oneidensis an arginine in the equivalent position is rhamnosylated. Inactivation of EF- P, or the corresponding modification systems, reduces not only bacterial fitness, but also impairs virulence. Here, we review the function of EF- P and IF-5 A and their unusual posttranslational protein modifications.
- Subjects
POLYPROLINE; ELONGATION factors (Biochemistry); GENETIC translation; PROTEIN synthesis; RNA-binding proteins
- Publication
Molecular Microbiology, 2016, Vol 99, Issue 2, p219
- ISSN
0950-382X
- Publication type
Article
- DOI
10.1111/mmi.13233