1993
DOI: 10.1099/00221287-139-12-3099
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Thermosensitive cell growth mutants of Enterococcus hirae that elongate at non-permissive temperature are stimulated to divide by parental autolytic enzymes

Abstract: ~ ~ ~~~A series of thermosensitive cell growth mutants of Enterococcus hirae have been isolated. Most of these mutants elongate and some show reduced autolytic activity when incubated at the non-permissive temperature (42 "C) in comparison to the wild-type incubated at the same temperature. When mutants were incubated for longer than 15 min at 42 "C and were then shifted to 30 "C, a lag proportional to the time of preincubation at 42 "C was observed before division, indicating that a certain time is necessary … Show more

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Cited by 3 publications
(3 citation statements)
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“…The majority of the chains of TX5127 had 2 to 10 cells per chain, while OG1RF mainly existed as single cells. Morphological change in E. hirae has been previously reported by Lleò et al for thermosensitive mutants, which showed great reduction in the production of muramidase-1 and formed elongated cells at nonpermissive temperature (19). Llèo et al postulated that muramidase-1 might be associated with the formation of septa, while muramidase-2 might be involved in separation of daughter cells.…”
Section: Resultsmentioning
confidence: 66%
“…The majority of the chains of TX5127 had 2 to 10 cells per chain, while OG1RF mainly existed as single cells. Morphological change in E. hirae has been previously reported by Lleò et al for thermosensitive mutants, which showed great reduction in the production of muramidase-1 and formed elongated cells at nonpermissive temperature (19). Llèo et al postulated that muramidase-1 might be associated with the formation of septa, while muramidase-2 might be involved in separation of daughter cells.…”
Section: Resultsmentioning
confidence: 66%
“…The second enzyme, peptidoglycan hydrolase-2, or muramidase-2, is found in the culture medium during cell growth and is active on cell walls of M. luteus and purified peptidoglycan of E. hirae (5, 11). It has been postulated that muramidase-2 may operate in conjunction with muramidase-1 in peptidoglycan hydrolysis (2) and may facilitate cell separation (14,24). The E. hirae muramidase-2 gene has recently been cloned and sequenced (3,9).…”
mentioning
confidence: 99%
“…One of these genes (arpU), which encoded a 15.9-kDa protein, was shown to complement the defect of the A9 mutant in trans. We propose that this gene may be involved in the regulation of muramidase-2 export.Peptidoglycan hydrolases are enzymes responsible for a number of important biological functions such as cell wall growth, cell separation, peptidoglycan turnover, competence for genetic transformation, sporulation, and bacteriolysis induced by beta-lactam antibiotics (7,8,14,21,23,27). Regulation of autolysin activity is believed to occur mostly at the posttranslational level.…”
mentioning
confidence: 99%