Compartmentalization of murein hydrolases in the envelope of <i>Escherichia coli</i>

Hakenbeck, R; Goodell, E. W.; Schwarz, Uli

doi:10.1016/0014-5793(74)80240-1

Cited by 22 publications

(11 citation statements)

References 20 publications

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“…Posttranslational regulatory mechanisms of these enzymes have been proposed to include (i) the activation of enzyme activity as a result of substrate modification (90,255), (ii) sequestration within lipid membranes (102,114), (iii) controlled transport across the cytoplasmic membrane (21), and (iv) topographical control within the peptidoglycan. The latter relies on evidence suggesting a multilayered arrangement of the peptidoglycan (113,204,225) in which the outside, unstressed layers would be susceptible to murein hydrolase activity, leaving the inner, load-bearing layers intact.…”

Section: Murein Hydrolasesmentioning

confidence: 99%

Molecular Control of Bacterial Death and Lysis

Rice

Bayles

2008

Microbiol Mol Biol Rev

319

312

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SUMMARY Although the phenomenon of bacterial cell death and lysis has been studied for over 100 years, the contribution of these important processes to bacterial physiology and development has only recently been recognized. Contemporary study of cell death and lysis in a number of different bacteria has revealed that these processes, once thought of as being passive and unregulated, are actually governed by highly complex regulatory systems. An emerging paradigm in this field suggests that, analogous to programmed cell death in eukaryotes, regulated cell death and lysis in bacteria play an important role in both developmental processes, such as competence and biofilm development, and the elimination of damaged cells, such as those irreversibly injured by environmental or antibiotic stress. Further study in this exciting field of bacterial research may provide new insight into the potential evolutionary link between control of cell death in bacteria and programmed cell death (apoptosis) in eukaryotes.

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Section: Murein Hydrolasesmentioning

confidence: 99%

Molecular Control of Bacterial Death and Lysis

Rice

Bayles

2008

Microbiol Mol Biol Rev

319

312

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“…Endopeptidase and carboxypeptidase activities were measured according to Hakenbeck et al [13]. Amidase was measured essentially as described by Pelzer [14].…”

Section: Assays Oj Murein Hydrolase Activitiesmentioning

confidence: 99%

“…2) within the cell envelope : transglycosylase [7], amidase [14,19], endopeptidase [12,14] and carboxypeptidase [9]. Endopeptidase and carboxypeptidase activities are found almost exclusively in the inner cytoplasmic membrane [13,15].…”

Section: Murein Synthesismentioning

confidence: 99%

Enzymes Synthesizing and Hydrolyzing Murein in Escherichia coli

Goodell

Schwarz

1977

European Journal of Biochemistry

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Envelopes from regions of the cell which in vivo show very little, if any, murein synthesis were isolated using the minicell-producing strain P678-54. Envelopes from minicells, representing in fact cell ends, were able to synthesize murein and to carry out transpeptidation in vitro; also all four murein hydrolase activities tested, carboxypeptidase, endopeptidase, amidase and transglycosylase, were found to be present. The specific activities of the murein synthesizing and degrading enzymes in envelopes derived from cell poles and from actively growing cells were similar. The topological distribution of murein-synthesizing enzymes and of murein hydrolases over the cell envelope is discussed.

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“…In adldition, it is exceptional in being inhibited by single-strandetl tleoxyribonucleic acid aild by some polynucleotides. The possible role of the enzymne in cell div-ision is discussed.Hydrolytic enzymes (1,2,6,11,12,18) participate in the metabolism of nmurein sacculi (21) and uindoubtedly p)lay a role in the maintenance of bacterial cell shape. In Escherichia coli, however, the precise biological role of the many murein hydrolases which have been identified remains largely obscure.…”

mentioning

confidence: 99%

“…Hydrolytic enzymes (1,2,6,11,12,18) participate in the metabolism of nmurein sacculi (21) and uindoubtedly p)lay a role in the maintenance of bacterial cell shape. In Escherichia coli, however, the precise biological role of the many murein hydrolases which have been identified remains largely obscure.…”

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confidence: 99%

Escherichia coli murein-DD-endopeptidase insensitive to beta-lactam antibiotics

Keck¹,

Schwarz²

1979

J Bacteriol

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A novel endopeptidase degrading the pel)tide cross-links in sacculi has been isolated from Escherichia coli and purified to homogeneity. I'lhe enzyme has a molecular weight of 30,000 and, in contrast to already known enzymes of similar specificity, remains fully active in the presence of/3-lactam antibiotics. In adldition, it is exceptional in being inhibited by single-strandetl tleoxyribonucleic acid aild by some polynucleotides. The possible role of the enzymne in cell div-ision is discussed.Hydrolytic enzymes (1,2,6,11,12,18) participate in the metabolism of nmurein sacculi (21) and uindoubtedly p)lay a role in the maintenance of bacterial cell shape. In Escherichia coli, however, the precise biological role of the many murein hydrolases which have been identified remains largely obscure. Among these enzymes, endopeptidases split peptide bridges cross-linking the glycan chains of murein and ar-e strongly inhibited by penicillins, although they are not assumed to be the lethal targets of /3-lactan antibiotics (5,9). I)uring purification of a l)enicillin-sensitive Dr-endopeptidase found to be identical with D-alanine-carboxypeptidase IB (18), we found a novel species of DD-endopeptidase which was totally insensitive to p)enicillin G; some prol)erties of the enzyme have been described previously (20; U. Schwarz, W. Keck, S. Klencke, and H. Mett, Abstr. Svmnip. Finctions Microb. Membranes, 1977). The enzyme thus belongs to a class of hydrolases which remain active in the presence of penicillin and mav be the cause of pericillin-in(duced cell lvsis.In this paper we report on the purification to homogeneity and the p)roperties of the novel endopeptidase. This enzyme is interesting not only because of its biological function but also because it has already been proven to be a powerful analytical tool; we have used it to elucidate the arrangement of the glycan chains within macromolectular sacculi (20). MATERIALS AND METHODSCell extraction and initial enrichment of endopeptidase. The enizyme was isolated fromii E. colli IPA 3092 (14) (iprn Iys), harvested at mid-exponential growth phase, aindl kept frozein at -70C. Cells (2(10 g, wet weight) were openied by shaking with glass beads in a tell mill in 500 mlt of Tris-miialeate (10 imiM; pH (6.8)-10 nmM MgSOi, containing 4(0 pg of DNase per ml (from bovine panc reas -450 Ktnit.z uInits per nmg, Serva). lThe filteired suspeiision (4) was cetntrifuged (6(1 mtmi at 48,0()) x g), the supernatant was (lialyzed three tiies againlst 5 litei-s Of 1'ris-miialeate htffer (1(1 mlM: pHI 5.2). 10 nmM MgSO, and 0.1 miiM dithioetrthritol, cleared by cntitl iftigatioIn (3(1 mIi, 28,0(1 X g (,aid aplplied On a (-olumn (2.6 h)y 31 (cmt; flow rate, :32 mIl/h) of CM Sepharose (I,-6B (IPharmacia Fine Chemiicals eqLilibrated with dialsis btuffer. T'he colunm was eluted with a (ont aeB giadtient (1380 ml of equilibration buffer, :120 ml of 0.5 M KCI in the sainet buffer).En(lopepti(lase was foundl in a hroatd p)eak letwe1tn ().andl (1.3 M K(CI The pooled fraot-tions with endopeptidase were ...

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Compartmentalization of murein hydrolases in the envelope of Escherichia coli

Cited by 22 publications

References 20 publications

Molecular Control of Bacterial Death and Lysis

Molecular Control of Bacterial Death and Lysis

Enzymes Synthesizing and Hydrolyzing Murein in Escherichia coli

Escherichia coli murein-DD-endopeptidase insensitive to beta-lactam antibiotics

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