FemABX Peptidyl Transferases: a Link between Branched-Chain Cell Wall Peptide Formation and β-Lactam Resistance in Gram-Positive Cocci

Rohrer, Susanne; Berger‐Bächi, Brigitte

doi:10.1128/aac.47.3.837-846.2003

Cited by 107 publications

(107 citation statements)

References 120 publications

(101 reference statements)

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“…3) include the Fem proteins, which utilize aa-tRNAs to synthesize a connecting peptide to bridge peptidoglycan chains. 42 This bridging peptide exhibits up to 5 aa. Depending on the bacterial species, the connecting peptide can be made of Gly, Ala, Ser, or Thr.…”

Section: The Cytosolic Domain Of Aapgs Exhibits a Gcn5-like Acetyltramentioning

confidence: 99%

“…This pathway is an alternate route to the direct bridging of peptidoglycan chains, and uses a set of penicillin binding proteins exhibiting a low affinity for β-lactam antibiotics (e.g., protein mecA in methicillin resistant S. aureus ). 42 Another family of tRNA-dependent enzymes exhibiting a GNAT fold are Arg- and Leu/Phe-transferases, which transfer Arg, Leu, or Phe to the N-termini of proteins, thereby targeting them for degradation via the ClpS-ClpXP-mediated N-end rule pathway (see [44] for review). The GNAT fold was recently identified in many more tRNA-dependent transferases in Streptomyces species, which utilize specific aa-tRNAs for synthesis of broad-spectrum antibiotics.…”

Section: The Cytosolic Domain Of Aapgs Exhibits a Gcn5-like Acetyltramentioning

confidence: 99%

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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: The Cytosolic Domain Of Aapgs Exhibits a Gcn5-like Acetyltramentioning

confidence: 99%

Section: The Cytosolic Domain Of Aapgs Exhibits a Gcn5-like Acetyltramentioning

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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“…1) (25). The catalytic activity of the transferases has been assessed only of purified FemX Wv from Weissella viridescens (26,27) and the Bpp transferases from E. faecalis (14,28).…”

Section: Discussionmentioning

confidence: 99%

Synthesis of Mosaic Peptidoglycan Cross-bridges by Hybrid Peptidoglycan Assembly Pathways in Gram-positive Bacteria

Arbeloa

Hugonnet

Sentilhes

et al. 2004

Journal of Biological Chemistry

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The peptidoglycan cross-bridges of Staphylococcus aureus, Enterococcus faecalis, and Enterococcus faecium consist of the sequences Gly 5 , L-Ala 2 , and D-Asx, respectively. Expression of the fmhB, femA, and femB genes of S. aureus in E. faecalis led to the production of peptidoglycan precursors substituted by mosaic side chains that were efficiently used by the penicillin-binding proteins for cross-bridge formation. The Fem transferases were specific for incorporation of glycyl residues at defined positions of the side chains in the absence of any additional S. aureus factors such as tRNAs used for amino acid activation. The PBPs of E. faecalis displayed a broad substrate specificity because mosaic side chains containing from 1 to 5 residues and Gly instead of L-Ala at the N-terminal position were used for peptidoglycan cross-linking. Low affinity PBP2a of S. aureus conferred ␤-lactam resistance in E. faecalis and E. faecium, thereby indicating that there was no barrier to heterospecific expression of resistance caused by variations in the structure of peptidoglycan precursors. Thus, conservation of the structure of the peptidoglycan cross-bridges in members of the same species reflects the high specificity of the enzymes for side chain synthesis, although this is not essential for the activity of the PBPs.

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“…4. Dendrogram of the FemABX protein family adapted from Rohrer & Berger-Bä chi (2003). Protein sequences were aligned using CLUSTAL W (Thompson et al, 1994) and the dendrogram was constructed using TREEVIEW (Page, 1996).…”

Section: Discussionmentioning

confidence: 99%

Application of a bacterial two-hybrid system for the analysis of protein–protein interactions between FemABX family proteins

Rohrer

Berger‐Bächi

2003

Microbiology

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Protein–protein interactions play an important role in all cellular processes. The development of two-hybrid systems in yeast and bacteria allows for in vivo assessment of such interactions. Using a recently developed bacterial two-hybrid system, the interactions of the Staphylococcus aureus proteins FemA, FemB and FmhB, members of the FemABX protein family, which is involved in peptidoglycan biosynthesis and β-lactam resistance of numerous Gram-positive bacteria, were analysed. While FmhB is involved in the addition of glycine 1 of the pentaglycine interpeptide of S. aureus peptidoglycan, FemA and FemB are specific for glycines 2/3 and 4/5, respectively. FemA–FemA, FemA–FemB and FemB–FemB interactions were found, while FmhB exists solely as a monomer. Interactions detected by the bacterial two-hybrid system were confirmed using the glutathione S-transferase-pulldown assay and gel filtration.

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FemABX Peptidyl Transferases: a Link between Branched-Chain Cell Wall Peptide Formation and β-Lactam Resistance in Gram-Positive Cocci

Cited by 107 publications

References 120 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

Synthesis of Mosaic Peptidoglycan Cross-bridges by Hybrid Peptidoglycan Assembly Pathways in Gram-positive Bacteria

Application of a bacterial two-hybrid system for the analysis of protein–protein interactions between FemABX family proteins

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