The Escherichia coli lov gene product connects peptidoglycan synthesis, ribosomes and growth rate.

Bouloc, Philippe; Jaffé, A; D’Ari, Richard

doi:10.1002/j.1460-2075.1989.tb03379.x

Cited by 36 publications

(20 citation statements)

References 50 publications

(23 reference statements)

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“…Additionally, the product of the lee gene helps coordinate the translational apparatus with the peptidoglycan synthetic machinery [50]. Therefore, control by growth rate could be exerted by mechanisms that monitor either the ribosomes or the peptidoglycan.…”

Section: Unifyin(} Perspectivementioning

confidence: 99%

Coordinate regulation of murein peptidase activity and AmpC β‐lactamase synthesis in Escherichia coli

Bishop¹,

Weiner²

1992

FEBS Letters

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In the periplasmic space of F.sche~'ichia coil, the (L)-m-A,pm-(D)-m-A,pm pcptid¢, the lipoprotein, and the AmpC fl-lactamas¢ are controlled by growth rate. To explain this coordinate regulation, it is proposed that the AmpC protein functions as an LD-endopeptidase in addition to its known function as a fl-lactamas¢. As LD-peptides, vo-peptides and fl-lactams are structurally similar, to-peptidases may belong to the larger family of DD-peptidases and serine ~-lactamases. In contrast to K coll. many related bacteria possess an inducible AmpC protein. Several gene systems necessary for AmpC induction are known to affect various aspects of peptidoglyean metabolism, It is proposed that AmpC induction ¢o=urs indirectly via a recyclabl¢ e¢ll wall pcptid¢.

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Section: Unifyin(} Perspectivementioning

confidence: 99%

Coordinate regulation of murein peptidase activity and AmpC β‐lactamase synthesis in Escherichia coli

Bishop¹,

Weiner²

1992

FEBS Letters

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“…One class consists of mutants which remain rod shaped in the absence of mecillinam but grow as spheres in its presence. These include aminoacyl-tRNA synthetase mutants, partially defective in aminoacylation (7,62), and cya and crp mutants (2,23), defective for the cyclic AMP (cAMP)-catabolite gene activator protein (CAP) complex, a transcriptional regulator (58). A second class consists of mutants which grow as spheres even in the absence of mecillinam; they are mutated at the mre locus (65)(66)(67).…”

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confidence: 99%

Mecillinam resistance in Escherichia coli is conferred by loss of a second activity of the AroK protein

et al. 1996

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Mecillinam, a ␤-lactam antibiotic specific to penicillin-binding protein 2 (PBP 2) in Escherichia coli, blocks cell wall elongation and, indirectly, cell division, but its lethality can be overcome by increased levels of ppGpp, the nucleotide effector of the stringent response. We have subjected an E. coli K-12 strain to random insertional mutagenesis with a mini-Tn10 element. One insertion, which was found to confer resistance to mecillinam in relA ؉ and relA strains, was mapped at 75.5 min on the E. coli map and was located between the promoters and the coding sequence of the aroK gene, which codes for shikimate kinase I, one of two E. coli shikimate kinases, both of which are involved in aromatic amino acid biosynthesis. The mecillinam resistance conferred by the insertion was abolished in a ⌬relA ⌬spoT strain completely lacking ppGpp, and it thus depends on the presence of ppGpp. Furthermore, the insertion increased the ppGpp pool approximately twofold in a relA ؉ strain. However, this increase was not observed in relA strains, although the insertion still conferred mecillinam resistance in these backgrounds, showing that mecillinam resistance is not due to an increased ppGpp pool. The resistance was also abolished in an ftsZ84(Ts) strain under semipermissive conditions, and the aroK::mini-Tn10 allele partially suppressed ftsZ84(Ts); however, it did not increase the concentration of the FtsZ cell division protein. The insertion greatly decreased or abolished the shikimate kinase activity of AroK in vivo and in vitro. The two shikimate kinases of E. coli are not equivalent; the loss of AroK confers mecillinam resistance, whereas the loss of AroL does not. Furthermore, the ability of the aroK mutation to confer mecillinam resistance is shown to be independent of polar effects on operon expression and of effects on the availability of aromatic amino acids or shikimic acid. Instead, we conclude that the AroK protein has a second activity, possibly related to cell division regulation, which confers mecillinam sensitivity. We were able to separate the AroK activities mutationally with an aroK mutant allele lacking shikimate kinase activity but still able to confer mecillinam sensitivity.

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“…It has been reported that cya and crp mutants, lacking a functional cyclic AMP-catabolite gene activator protein complex, have this phenotype (3,23); the amdinocillin resistance of these mutants, however, seems to depend on the genetic background (reference 11 and unpublished results). Aminoacyl-tRNA synthetase mutants also belong to this class (6,52). These enzymes charge amino acids on their respective tRNAs.…”

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confidence: 99%

Penicillin-binding protein 2 inactivation in Escherichia coli results in cell division inhibition, which is relieved by FtsZ overexpression

et al. 1993

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Aminoacyl-tRNA synthetase mutants of Escherichia coli are resistant to amdinocillin (mecillinam), a P-lactam antibiotic which specifically binds penicillin-binding protein 2 (PBP2) and prevents cell wall elongation with concomitant cell death. The leuS(Ts) strain, in which leucyl-tRNA synthetase is temperature sensitive, was resistant to amdinocillin at 37°C because of an increased guanosine 5'-diphosphate 3'-diphosphate (ppGpp) pool resulting from partial induction of the stringent response, but it was sensitive to amdinocillin at 25°C. We constructed a leuS(Ts) A(rod4-pbpA)::KMr strain, in which the PBP2 structural gene is deleted. This strain grew as spherical cells at 37°C but was not viable at 25°C. After a shift from 37 to 25°C, the ppGpp pool decreased and cell division was inhibited; the cells slowly carried out a single division, increased considerably in volume, and gradually lost viability. The cell division inhibition was reversible when the ppGpp pool increased at high temperature, but reversion required de novo protein synthesis, possibly of septation proteins. The multicopy plasmid pZAQ, overproducing the septation proteins FtsZ, FtsA, and FtsQ, conferred amdinocillin resistance on a wild-type strain and suppressed the cell division inhibition in the leuS(Ts) A(rodA-pbpA)::KMr strain at 25°C. The plasmid pAQ, in which theftsZ gene is inactivated, did not confer amdinocillin resistance. These results lead us to hypothesize that the nucleotide ppGpp activatesftsZ expression and thus couples cell division to protein synthesis.

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The Escherichia coli lov gene product connects peptidoglycan synthesis, ribosomes and growth rate.

Cited by 36 publications

References 50 publications

Coordinate regulation of murein peptidase activity and AmpC β‐lactamase synthesis in Escherichia coli

Coordinate regulation of murein peptidase activity and AmpC β‐lactamase synthesis in Escherichia coli

Mecillinam resistance in Escherichia coli is conferred by loss of a second activity of the AroK protein

Penicillin-binding protein 2 inactivation in Escherichia coli results in cell division inhibition, which is relieved by FtsZ overexpression

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