The participation of sRNA in the enzymatic synthesis of O-L-lysyl phosphatidylgylcerol in Staphylococcus aureus.

Lennarz, William J.; Nesbitt, John A.; Reiss, J

doi:10.1073/pnas.55.4.934

Cited by 72 publications

(41 citation statements)

References 10 publications

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“…20,21 The bacterial enzyme responsible for synthesis of Lys-PG was not determined until 40 y later during a genetic screen aimed at identifying mutants of S. aureus that are sensitive to CAMPs. 22 Peschel and coauthors were the first to establish that lysyl-PG synthase (LysPGS), encoded by the gene mprF ( m ultiple p eptide r esistance f actor), enhances resistance of S. aureus to 10 CAMPs from various origins.…”

Section: Trna-dependent Aminoacylation Of Membrane Phosphatidylglycerolmentioning

confidence: 99%

Deciphering the tRNA-dependent lipid aminoacylation systems in bacteria: Novel components and structural advances

Fields

Roy

2017

RNA Biology

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ABSTRACTtRNA-dependent addition of amino acids to lipids on the outer surface of the bacterial membrane results in decreased effectiveness of antimicrobials such as cationic antimicrobial peptides (CAMPs) that target the membrane, and increased virulence of several pathogenic species. After a brief introduction to CAMPs and the various bacterial resistance mechanisms used to counteract these compounds, this review focuses on recent advances in tRNA-dependent pathways for lipid modification in bacteria. Phenotypes associated with amino acid lipid modifications and regulation of their expression will also be discussed.

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Section: Trna-dependent Aminoacylation Of Membrane Phosphatidylglycerolmentioning

confidence: 99%

Deciphering the tRNA-dependent lipid aminoacylation systems in bacteria: Novel components and structural advances

Fields

Roy

2017

RNA Biology

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“…modification of lipid A with 4-amino-4-deoxy-L-arabinose), iii) biosynthesis of phosphatidylethanolamine (PE) (3) and iv) lysylation of phosphatidylglycerol (PG) (4). PG lysylation activity, first discovered in Staphylococcus aureus (5), involves transfer of a Lys moiety from the 3'-end of tRNA Lys to the free distal hydroxyl group of the glycerol moiety of PG (6,7). The specificity of the staphylococcal protein was investigated, showing that the Lys analog S-(2-aminoethyl)-l-cysteine can be efficiently processed when attached to E. coli tRNA Lys but not tRNA Cys (7).…”

Section: Introductionmentioning

confidence: 99%

Monitoring Lys-tRNALys phosphatidylglycerol transferase activity

Roy

Ibba

2008

Methods

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In some bacteria Lys-tRNA Lys is used both in translation and for the specific addition of Lys to phosphatidylglycerol in the cytoplasmic membrane. This reaction is catalyzed by the membrane protein MprF, and the lysyl-phosphatidylglycerol formed contributes to the resistance of these bacteria to various cationic antibacterial molecules. Obtaining proteins and reconstituting an in vitro system mimicking membrane conditions is a major challenge to studying the function of membrane proteins, especially when labile substrates such as Lys-tRNA Lys are required. Here we report methods to obtain a stable enriched membrane fraction containing MprF, and the techniques necessary to quantitatively monitor its activity in vitro and in vivo.

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“…The remaining type of aa-tRNAs found in the cell consists of correctly charged species used for cellular processes other than translation. Examples are the porphyrin 'precursor' Glu-tRNA Glu (Schauer et al 2002), the cell wall peptidoglycan precursors Gly-tRNA Gly (Bumsted et al 1968) and Ser-tRNA Ser (Petit et al 1968), and the lysyl-phosphatidylglycerol precursor Lys-tRNA Lys (Lennarz et al 1966;Oku et al 2004). When these numerous aa-tRNAs are all taken into account in Escherichia coli, where the picture is perhaps most complete, it can be seen that a normally growing cell might contain 25 or more different types of aa-tRNAs.…”

Section: How Many Aa-trnas Are There?mentioning

confidence: 99%

Aminoacyl-tRNAs: setting the limits of the genetic code

Ibba¹,

Söll²

2004

Genes Dev.

151

117

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Aminoacyl-tRNAs (aa-tRNAs) are simple molecules with a single purpose-to serve as substrates for translation. They consist of mature tRNAs to which an amino acid has been esterified at the 3Ј-end. The 20 different types of aa-tRNA are made by the 20 different aminoacyl-tRNA synthetases (aaRSs, of which there are two classes), one for each amino acid of the genetic code . This would be fine if it were not for the fact that such a straightforward textbook scenario is not true in a single known living organism. aa-tRNAs lie at the heart of gene expression; they interpret the genetic code by providing the interface between nucleic acid triplets in mRNA and the corresponding amino acids in proteins. The synthesis of aa-tRNAs impacts the accuracy of translation, the expansion of the genetic code, and even provides tangible links to primary metabolism. These central roles vest immense power in aa-tRNAs, and recent studies show just how complex and diverse their synthesis is.

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The participation of sRNA in the enzymatic synthesis of O-L-lysyl phosphatidylgylcerol in Staphylococcus aureus.

Cited by 72 publications

References 10 publications

Deciphering the tRNA-dependent lipid aminoacylation systems in bacteria: Novel components and structural advances

Deciphering the tRNA-dependent lipid aminoacylation systems in bacteria: Novel components and structural advances

Monitoring Lys-tRNALys phosphatidylglycerol transferase activity

Aminoacyl-tRNAs: setting the limits of the genetic code

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