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Lookup NU author(s): Professor Waldemar Vollmer
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Lytic transglycosylases are a unique lysozyme-like class of murein hydrolases believed to be important for growth of Escherichia coli. A membrane-bound lytic transglycosylase with an apparent molecular mass of 38 kDa, which was designated Mlt38, has previously been purified and characterized (A. Ursinus and J.-V. Holtje, J. Bacteriol. 176:338-343, 1994). On the basis of four tryptic peptides, the gene mltA was mapped at 63 min on the chromosomal map of E. coli K-12 and cloned by reverse genetics. The open reading frame was found to contain a typical lipoprotein consensus sequence, and the lipoprotein nature of the gene product was demonstrated by [3H]palmitate labeling. On the basis of the distribution of MltA in membrane fractions obtained by sucrose gradient centrifugation, a localization in the outer membrane is indicated. Overexpression of MltA at 30 degrees C, the optimal temperature for enzyme activity, but not at 37 degrees C results in the formation of spheroplasts. Not only a deletion mutant in mltA, but also double mutants in mltA and one of the two other well-characterized lytic transglycosylases (either sltY or mltB), as well as a triple mutant in all three enzymes, showed no obvious phenotype. However, dramatic changes in the structure of the murein sacculus indicate that lytic transglycosylases are involved in maturation of the murein sacculus.
Author(s): Lommatzsch J, Templin MF, Kraft AR, Vollmer W, Höltje J-V
Publication type: Article
Publication status: Published
Journal: Journal of Bacteriology
Year: 1997
Volume: 179
Issue: 17
Pages: 5465-5470
Print publication date: 01/09/1997
ISSN (print): 0021-9193
ISSN (electronic): 1067-8832
Publisher: American Society for Microbiology
URL: http://jb.asm.org/cgi/content/abstract/179/17/5465
