Switching the Post-translational Modification of Translation Elongation Factor EF-P.
EpmA
EarP
IF5A
NleB
Pseudomonas aeruginosa
TDP-rhamnose
bacterial two-hybrid
glycosylation
Journal
Frontiers in microbiology
ISSN: 1664-302X
Titre abrégé: Front Microbiol
Pays: Switzerland
ID NLM: 101548977
Informations de publication
Date de publication:
2019
2019
Historique:
received:
30
01
2019
accepted:
06
05
2019
entrez:
11
6
2019
pubmed:
11
6
2019
medline:
11
6
2019
Statut:
epublish
Résumé
Tripeptides with two consecutive prolines are the shortest and most frequent sequences causing ribosome stalling. The bacterial translation elongation factor P (EF-P) relieves this arrest, allowing protein biosynthesis to continue. A seven amino acids long loop between beta-strands β3/β4 is crucial for EF-P function and modified at its tip by lysylation of lysine or rhamnosylation of arginine. Phylogenetic analyses unveiled an invariant proline in the -2 position of the modification site in EF-Ps that utilize lysine modifications such as
Identifiants
pubmed: 31178848
doi: 10.3389/fmicb.2019.01148
pmc: PMC6544042
doi:
Types de publication
Journal Article
Langues
eng
Pagination
1148Références
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