Controlling Autolysis During Flagella Insertion in Gram-Negative Bacteria

Herlihey, Francesca A.; Clarke, Anthony J.

doi:10.1007/5584_2016_52

Cited by 33 publications

(44 citation statements)

References 88 publications

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“…Six unique LT catalytic folds are known in Gram-negative bacteria, with each annotated as a conserved domain in the Pfam database (Figure 3). These six domains were organized previously into six distinct families (Herlihey & Clarke, 2016). LTs may be further organized by their substrate preference for either exolytic or endolytic strand cleavage.…”

Section: A Large Diverse Family Of Lts Has Evolvedmentioning

confidence: 99%

“…Further studies revealed that SltF interacts with FlgJ to excavate the cell wall for the insertion of the flagellum protein edifice through the sacculus (de la Mora et al , 2007). Herlihey and Clarke assigned SltF to the new subfamily 1F of Family 1 based on sequence analysis (Herlihey & Clarke, 2016). The Pfam database recognizes the catalytic domain of SltF as a Family 1 SLT domain (Pfam: PF01464).…”

Section: Gram-negative Family 1 Lytic Transglycosylasesmentioning

confidence: 99%

“…As noted earlier, the glutamate in Motif I of R. sphaeroides SltF is flanked by a threonine rather than a serine. Homologous SltF proteins in other Gram-negative organisms retain the more common ES Motif I (Herlihey & Clarke, 2016). The E57A and E83A mutants of SltF lacked activity (de la Mora et al , 2007).…”

Section: Gram-negative Family 1 Lytic Transglycosylasesmentioning

confidence: 99%

“…It has long been believed that LTs function in the chain termination of nascent peptidoglycan, given the relative scarcity of reducing saccharide termini in muropeptides obtained from amidase-catalyzed degradation of sacculi. The seven consensus motifs of the Family 5 LTs are Motif I (residues K–X 7 –G–T–Y); Motif II (L–X 4 –G–K–E–X–Q–X 6 –E–G); Motif III (E–G–X 3 –P–X–T–X 2 –Y–X 5 –D–X 3 –L–X); Motif IV (A–S–I–X–E–K–E); Motif V (E–R–X 2 –V–X–S–V–F–X 2 –N–R–L–X 3 –M–X–L–Q–T–D–V–I–Y–G–X–g); Motif VI (G–X 5 –D–L–X 5 –Y–N–T–Y–X–I–X–G–L–P–P); and Motif VII (L–X–A–X–A–X–P–X 2 –T–X 3 –Y–F–V–A–D–G–X 3 –G–G–H–X–F–X–L–X 2 –H–N) (Herlihey & Clarke, 2016). The catalytic glutamate in Motif IV is preceded by a conserved EK pair and is followed commonly by a threonine residue (Figure 12), similar to Family 3 LTs.…”

Section: Gram-negative Family 5 Lytic Transglycosylasesmentioning

confidence: 99%

“…This review discusses first the reaction products of LT catalysis, and progresses to the protein structural studies that organize the LT superfamily of the Gram-negative bacteria. We expand the previous six-family classification for the Gram-negative LTs (Herlihey & Clarke, 2016) and introduce two new families to accommodate the Gram-positive LTs. This latter section comprises the major topic of this review.…”

Section: Introductionmentioning

confidence: 99%

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Lytic transglycosylases: concinnity in concision of the bacterial cell wall

Dik

Marous

Fisher

et al. 2017

Critical Reviews in Biochemistry and Molecular Biology

135

188

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The lytic transglycosylases (LTs) are bacterial enzymes that catalyze the non-hydrolytic cleavage of the peptidoglycan structures of the bacterial cell wall. They are not catalysts of glycan synthesis as might be surmised from their name. Notwithstanding the seemingly mundane reaction catalyzed by the LTs, their lytic reactions serve bacteria for a series of astonishingly diverse purposes. These purposes include cell-wall synthesis, remodeling, and degradation; for the detection of cell-wall-acting antibiotics; for the expression of the mechanism of cell-wall-acting antibiotics; for the insertion of secretion systems and flagellar assemblies into the cell wall; as a virulence mechanism during infection by certain Gram-negative bacteria; and in the sporulation and germination of Gram-positive spores. Significant advances in the mechanistic understanding of each of these processes have coincided with the successive discovery of new LTs structures. In this review, we provide a systematic perspective on what is known on the structure-function correlations for the LTs, while simultaneously identifying numerous opportunities for the future study of these enigmatic enzymes.

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Section: A Large Diverse Family Of Lts Has Evolvedmentioning

confidence: 99%

Section: Gram-negative Family 1 Lytic Transglycosylasesmentioning

confidence: 99%

Section: Gram-negative Family 1 Lytic Transglycosylasesmentioning

confidence: 99%

Section: Gram-negative Family 5 Lytic Transglycosylasesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Lytic transglycosylases: concinnity in concision of the bacterial cell wall

Dik

Marous

Fisher

et al. 2017

Critical Reviews in Biochemistry and Molecular Biology

135

188

View full text Add to dashboard Cite

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Macromolecular Machineries in Cell‐Wall Recycling

Batuecas

Hermoso

2019

Encyclopedia of Life Sciences

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Peptidoglycan, the major constituent of bacterial cell wall, is a huge polymeric macromolecule composed of glycan strands covalently linked by interconnecting peptide stems and critical for survival of bacteria. Peptidoglycan is constantly edited, biosynthesised and degraded, during essential bacterial processes such as division, elongation or insertion of the cellular machinery (e.g. flagella, pili) into cell wall. Degradation fragments are recovered, especially in Gram‐negative bacteria, by active transport and recycled to rebuild the wall. In some important Gram‐negative pathogens, β‐lactam resistance is directly linked to peptidoglycan recycling. The recycling process requires orchestration of different lytic enzymes and transporters from periplasm, the inner membrane, to cytoplasm. Recent structural and functional studies have provided relevant insights into enzymatic regulation, substrate specificity and activity of the lytic machineries involved in recycling with relevant implications in antibiotics resistance. Key Concepts Peptidoglycan recycling is an essential process in Gram‐negative bacteria that recovers self‐degradation products of cell wall in the cytoplasm to reutilise them to rebuild the wall. PG recycling is important in cell‐wall biosynthesis and in bacterial communication in many bacteria, and in antibiotics resistance in some pathogens from Enterobacteriaceae and Pseudomonadaceae families. PG recycling involves a large number of enzymes and transporters spanning from periplasm, inner and outer membranes, and cytoplasm. Lytic transglycosylases (LTs) are periplasmic and, typically, modular enzymes that initiate PG recycling by non‐hydrolytic degradation of glycan chains. They are classified in six families. Several LTs are found in each Gram‐negative bacterium. The Slt structure reveals how, under the effect of β‐lactam antibiotics, the cell wall is repaired by degradation of aberrant nascent PG chains and how it initiates the resistance phenotype. MltF is a modular membrane‐bound LT that experiences allosteric activation triggered by muropeptides. PG amidases are present in periplasm and cytoplasm. Activity in periplasm is regulated by cellular location, protein–protein interactions and oligomeric state. An activation mechanism has been discovered for cytosolic enzymes. Anhydro‐muropeptides are the key molecules to activate the AmpR to induce AmpC β‐lactamase in response to β‐lactam challenge. Regulation (in space and time) of the catalytic processes as well as of interaction between different partners is essential in PG recycling enzymes.

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