Partition of tRNAGly isoacceptors between protein and cell-wall peptidoglycan synthesis in Staphylococcus aureus.


Journal

Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011

Informations de publication

Date de publication:
25 01 2021
Historique:
accepted: 09 12 2020
revised: 04 12 2020
received: 30 04 2020
pubmed: 29 12 2020
medline: 9 2 2021
entrez: 28 12 2020
Statut: ppublish

Résumé

The sequence of tRNAs is submitted to evolutionary constraints imposed by their multiple interactions with aminoacyl-tRNA synthetases, translation elongation factor Tu in complex with GTP (EF-Tu•GTP), and the ribosome, each being essential for accurate and effective decoding of messenger RNAs. In Staphylococcus aureus, an additional constraint is imposed by the participation of tRNAGly isoacceptors in the addition of a pentaglycine side chain to cell-wall peptidoglycan precursors by transferases FmhB, FemA and FemB. Three tRNAGly isoacceptors poorly interacting with EF-Tu•GTP and the ribosome were previously identified. Here, we show that these 'non-proteogenic' tRNAs are preferentially recognized by FmhB based on kinetic analyses and on synthesis of stable aminoacyl-tRNA analogues acting as inhibitors. Synthesis of chimeric tRNAs and of helices mimicking the tRNA acceptor arms revealed that this discrimination involves identity determinants exclusively present in the D and T stems and loops of non-proteogenic tRNAs, which belong to an evolutionary lineage only present in the staphylococci. EF-Tu•GTP competitively inhibited FmhB by sequestration of 'proteogenic' aminoacyl-tRNAs in vitro. Together, these results indicate that competition for the Gly-tRNAGly pool is restricted by both limited recognition of non-proteogenic tRNAs by EF-Tu•GTP and limited recognition of proteogenic tRNAs by FmhB.

Identifiants

pubmed: 33367813
pii: 6047289
doi: 10.1093/nar/gkaa1242
pmc: PMC7826273
doi:

Substances chimiques

Bacterial Proteins 0
FemA protein, Bacteria 0
FemB protein, methicillin-resistant Staphylococcus aureus 0
Peptidoglycan 0
RNA, Bacterial 0
RNA, Transfer, Gly 0
Guanosine Triphosphate 86-01-1
Peptide Elongation Factor Tu EC 3.6.1.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

684-699

Informations de copyright

© The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.

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Auteurs

Lauriane Rietmeyer (L)

INSERM, Sorbonne Université, Université de Paris, Centre de Recherche des Cordeliers (CRC), F-75006 Paris, France.

Nicolas Fix-Boulier (N)

INSERM, Sorbonne Université, Université de Paris, Centre de Recherche des Cordeliers (CRC), F-75006 Paris, France.

Chloé Le Fournis (C)

INSERM, Sorbonne Université, Université de Paris, Centre de Recherche des Cordeliers (CRC), F-75006 Paris, France.

Laura Iannazzo (L)

Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques, Université de Paris, CNRS UMR 8601, Paris F-75006 France.

Camelia Kitoun (C)

Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques, Université de Paris, CNRS UMR 8601, Paris F-75006 France.

Delphine Patin (D)

Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198 Gif-sur-Yvette, France.

Dominique Mengin-Lecreulx (D)

Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198 Gif-sur-Yvette, France.

Mélanie Ethève-Quelquejeu (M)

Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques, Université de Paris, CNRS UMR 8601, Paris F-75006 France.

Michel Arthur (M)

INSERM, Sorbonne Université, Université de Paris, Centre de Recherche des Cordeliers (CRC), F-75006 Paris, France.

Matthieu Fonvielle (M)

INSERM, Sorbonne Université, Université de Paris, Centre de Recherche des Cordeliers (CRC), F-75006 Paris, France.

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Classifications MeSH