Identification and characterization of the Escherichia coli envC gene encoding a periplasmic coiled-coil protein with putative peptidase activity

原, 弘志

doi:10.1016/s0378-1097(02)00749-8

Cited by 17 publications

(50 citation statements)

References 23 publications

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“…The mutant showed hypersensitivity to dyes, a leakage of periplasmic proteins, and other defects indicating the perturbation of the outer membrane (121). Later, envC was recognized as the yibP open reading frame, and the single-residue substitution causing the mutation was identified (88).…”

Section: Penicillin-insensitive Peptidasesmentioning

confidence: 99%

“…The cleavage of the signal sequence yields a mature protein anchored to the cytoplasmic membrane, and a 43-kDa form is released upon spheroplast formation (88). The Nterminal half of the mature form is composed mostly of sequences with a repetitive pattern characteristic of a coiled-coil structure possibly involved in the oligomerization of EnvC or in its interaction with another protein (88).…”

Section: Penicillin-insensitive Peptidasesmentioning

confidence: 99%

“…The Nterminal half of the mature form is composed mostly of sequences with a repetitive pattern characteristic of a coiled-coil structure possibly involved in the oligomerization of EnvC or in its interaction with another protein (88). The activation of AmiA and AmiB by EnvC (273) suggests a possible protein-protein interaction between EnvC and these amidases.…”

Section: Penicillin-insensitive Peptidasesmentioning

confidence: 99%

“…The activation of AmiA and AmiB by EnvC (273) suggests a possible protein-protein interaction between EnvC and these amidases. The C-terminal domain of EnvC resembles a zinc metallopeptidase and has homology with the staphylococcal LytM lysostaphin, which is known to degrade PG cross-linkages (88). The PG hydrolase activity of EnvC was assessed by zymography (20).…”

Section: Penicillin-insensitive Peptidasesmentioning

confidence: 99%

“…The overexpression of envC leads to growth inhibition, morphological aberrations, and cell lysis (88,273). EnvC, together with three other LytM factors (NlpD, YgeR, and YebA) discovered in E. coli, is required for septal PG splitting and daughter cell separation (272).…”

Section: Penicillin-insensitive Peptidasesmentioning

confidence: 99%

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Peptidoglycan Hydrolases of Escherichia coli

Heijenoort

2011

Microbiol Mol Biol Rev

190

233

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SUMMARY The review summarizes the abundant information on the 35 identified peptidoglycan (PG) hydrolases of Escherichia coli classified into 12 distinct families, including mainly glycosidases, peptidases, and amidases. An attempt is also made to critically assess their functions in PG maturation, turnover, elongation, septation, and recycling as well as in cell autolysis. There is at least one hydrolytic activity for each bond linking PG components, and most hydrolase genes were identified. Few hydrolases appear to be individually essential. The crystal structures and reaction mechanisms of certain hydrolases having defined functions were investigated. However, our knowledge of the biochemical properties of most hydrolases still remains fragmentary, and that of their cellular functions remains elusive. Owing to redundancy, PG hydrolases far outnumber the enzymes of PG biosynthesis. The presence of the two sets of enzymes acting on the PG bonds raises the question of their functional correlations. It is difficult to understand why E. coli keeps such a large set of PG hydrolases. The subtle differences in substrate specificities between the isoenzymes of each family certainly reflect a variety of as-yet-unidentified physiological functions. Their study will be a far more difficult challenge than that of the steps of the PG biosynthesis pathway.

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Section: Penicillin-insensitive Peptidasesmentioning

confidence: 99%

Section: Penicillin-insensitive Peptidasesmentioning

confidence: 99%

Section: Penicillin-insensitive Peptidasesmentioning

confidence: 99%

Section: Penicillin-insensitive Peptidasesmentioning

confidence: 99%

Section: Penicillin-insensitive Peptidasesmentioning

confidence: 99%

See 3 more Smart Citations

Peptidoglycan Hydrolases of Escherichia coli

Heijenoort

2011

Microbiol Mol Biol Rev

190

233

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Daughter cell separation is controlled by cytokinetic ring-activated cell wall hydrolysis

Uehara

Parzych

Dinh

et al. 2010

EMBO J

307

459

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During bacterial cytokinesis, hydrolytic enzymes are used to split wall material shared by adjacent daughter cells to promote their separation. Precise control over these enzymes is critical to prevent breaches in wall integrity that can cause cell lysis. How these potentially lethal hydrolases are regulated has remained unknown. Here, we investigate the regulation of cell wall turnover at the Escherichia coli division site. We show that two components of the division machinery with LytM domains (EnvC and NlpD) are direct regulators of the cell wall hydrolases (amidases) responsible for cell separation (AmiA, AmiB and AmiC). Using in vitro cell wall cleavage assays, we show that EnvC activates AmiA and AmiB, whereas NlpD activates AmiC. Consistent with these findings, we show that an unregulated EnvC mutant requires functional AmiA or AmiB but not AmiC to induce cell lysis, and that the loss of NlpD phenocopies an AmiC À defect. Overall, our results suggest that cellular amidase activity is regulated spatially and temporally by coupling their activation to the assembly of the cytokinetic ring.

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An ATP-binding cassette transporter-like complex governs cell-wall hydrolysis at the bacterial cytokinetic ring

Yang

Peters

Parzych

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

193

255

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ATP-binding cassette transporters are ubiquitous membrane protein complexes that move substrates across membranes. They do so using ATP-induced conformational changes in their nucleotide-binding domains to alter the conformation of the transport cavity formed by their transmembrane domains. In Escherichia coli , an ATP-binding cassette transporter-like complex composed of FtsE (nucleotide-binding domain) and FtsX (transmembrane domain) has long been known to be important for cytokinesis, but its role in the process has remained mysterious. Here we identify FtsEX as a regulator of cell-wall hydrolysis at the division site. Cell-wall material synthesized by the division machinery is shared initially by daughter cells and must be split by hydrolytic enzymes called “amidases” to drive daughter-cell separation. We recently showed that the amidases require activation at the cytokinetic ring by proteins with LytM domains, of which EnvC is the most critical. In this report, we demonstrate that FtsEX directly recruits EnvC to the septum via an interaction between EnvC and a periplasmic loop of FtsX. Importantly, we also show that FtsEX variants predicted to be ATPase defective still recruit EnvC to the septum but fail to promote cell separation. Our results thus suggest that amidase activation via EnvC in the periplasm is regulated by conformational changes in the FtsEX complex mediated by ATP hydrolysis in the cytoplasm. Since FtsE has been reported to interact with the tubulin-like FtsZ protein, our model provides a potential mechanism for coupling amidase activity with the contraction of the FtsZ cytoskeletal ring.

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Identification and characterization of the Escherichia coli envC gene encoding a periplasmic coiled-coil protein with putative peptidase activity

Cited by 17 publications

References 23 publications

Peptidoglycan Hydrolases of Escherichia coli

Peptidoglycan Hydrolases of Escherichia coli

Daughter cell separation is controlled by cytokinetic ring-activated cell wall hydrolysis

An ATP-binding cassette transporter-like complex governs cell-wall hydrolysis at the bacterial cytokinetic ring

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