ArticleJournal of bacteriology1991
Subcellular distribution of the soluble lytic transglycosylase in Escherichia coli.
Article in Journal of bacteriology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 41 citations in OpenAlex.
- Lytic transglycosylase Slt of Pseudomonas aeruginosa as a periplasmic hub protein.Protein science : a publication of the Protein Society · 2024Article
- NlpI-Prc Proteolytic Complex Mediates Peptidoglycan Synthesis and Degradation via Regulation of Hydrolases and Synthases inInternational journal of molecular sciences · 2023Article
- The periplasmic HrpB1 protein from Xanthomonas spp. binds to peptidoglycan and to components of the type III secretion system.Applied and environmental microbiology · 2013Article
- Peptidoglycan hydrolases of Escherichia coli.Microbiology and molecular biology reviews : MMBR · 2011Review
- The C-terminal domain of Escherichia coli YfhD functions as a lytic transglycosylase.The Journal of biological chemistry · 2008Article
- Subcellular location of the soluble lytic transglycosylase homologue in Staphylococcus aureus.Current microbiology · 2005Article
- Membrane-bound lytic endotransglycosylase in Escherichia coli.Journal of bacteriology · 1998Article
- Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli.Microbiology and molecular biology reviews : MMBR · 1998Review
- Outer membrane localization of murein hydrolases: MltA, a third lipoprotein lytic transglycosylase in Escherichia coli.Journal of bacteriology · 1997Article
- A major autolysin of Pseudomonas aeruginosa: subcellular distribution, potential role in cell growth and division and secretion in surface membrane vesicles.Journal of bacteriology · 1996Article
- An autolysin ring associated with cell separation of Staphylococcus aureus.Journal of bacteriology · 1996Article
- Analysis of the sodium dodecyl sulfate-stable peptidoglycan autolysins of select gram-negative pathogens by using renaturing polyacrylamide gel electrophoresis.Journal of bacteriology · 1994Article
- Murein-metabolizing enzymes from Escherichia coli: existence of a second lytic transglycosylase.Journal of bacteriology · 1992Article
- A new mercury-penicillin V derivative as a probe for ultrastructural localization of penicillin-binding proteins in Escherichia coli.Journal of bacteriology · 1992Article
- Extracellular and cellular distribution of muramidase-2 and muramidase-1 of Enterococcus hirae ATCC 9790.Journal of bacteriology · 1992Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The localization of the major autolytic enzyme, the soluble lytic transglycosylase, in the different cell compartments of Escherichia coli was investigated by immunoelectron microscopy. Ultrathin sections were labeled with a specific antiserum against purified soluble lytic transglycosylase, and the antibody-enzyme complexes were visualized with colloidal protein A-gold. A preferential localization of the lytic transglycosylase in the envelope was observed, with only 20 to 30% of the enzyme left in the cytoplasm. Most of the enzyme associated with the cell wall was tightly bound to the murein sacculus. Sacculi prepared by boiling of cells in 4% sodium dodecyl sulfate could be immunolabeled with the specific antiserum, indicating a surprisingly strong interaction of the lytic transglycosylase with murein. The enzyme-substrate complex could be reconstituted in vitro by incubating pronase-treated, protein-free murein sacculi with purified lytic transglycosylase at 0 degrees C. Titration of sacculi with increasing amounts of enzyme indicated a limiting number of binding sites for about 1,000 molecules of enzyme per sacculus. Ruptured murein sacculi obtained after penicillin treatment revealed that the enzyme is exclusively bound to the outer surface of the sacculus. This finding is discussed in the light of recent evidence suggesting that the murein of E. coli might be a structure of more than one layer expanding by inside-to-outside growth of patches of murein.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.