Lytic transglycosylase MltG cleaves in nascent peptidoglycan and produces short glycan strands
Bacteria encase their cytoplasmic membrane with peptidoglycan (PG) to maintain the shape of the cell and protect it from bursting. The enlargement of the PG layer is facilitated by the coordinated activities of PG synthesising and -cleaving enzymes. In Escherichia coli, the cytoplasmic membrane-boun...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2021-12-01
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| Series: | The Cell Surface |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2468233021000062 |
| _version_ | 1818460092750626816 |
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| author | Jad Sassine Manuel Pazos Eefjan Breukink Waldemar Vollmer |
| author_facet | Jad Sassine Manuel Pazos Eefjan Breukink Waldemar Vollmer |
| author_sort | Jad Sassine |
| collection | DOAJ |
| description | Bacteria encase their cytoplasmic membrane with peptidoglycan (PG) to maintain the shape of the cell and protect it from bursting. The enlargement of the PG layer is facilitated by the coordinated activities of PG synthesising and -cleaving enzymes. In Escherichia coli, the cytoplasmic membrane-bound lytic transglycosylase MltG associates with PG synthases and was suggested to terminate the polymerisation of PG glycan strands. Using pull-down and surface plasmon resonance, we detected interactions between MltG from Bacillus subtilis and two PG synthases; the class A PBP1 and the class B PBP2B. Using in vitro PG synthesis assays with radio-labelled or fluorophore-labelled B. subtilis-type and/or E. coli-type lipid II, we showed that both, BsMltG and EcMltG, are lytic tranglycosylases and that their activity is higher during ongoing glycan strand polymerisation. MltG competed with the transpeptidase activity of class A PBPs, but had no effect on their glycosyltransferase activity, and produced glycan strands with a length of 7 disaccharide units from cleavage in the nascent strands. We hypothesize that MltG cleaves the nascent strands to produce short glycan strands that are used in the cell for a yet unknown process. |
| first_indexed | 2024-12-14T23:24:45Z |
| format | Article |
| id | doaj.art-5398c4d38ead4d34ae2d9e9755b8679a |
| institution | Directory Open Access Journal |
| issn | 2468-2330 |
| language | English |
| last_indexed | 2024-12-14T23:24:45Z |
| publishDate | 2021-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | The Cell Surface |
| spelling | doaj.art-5398c4d38ead4d34ae2d9e9755b8679a2022-12-21T22:43:50ZengElsevierThe Cell Surface2468-23302021-12-017100053Lytic transglycosylase MltG cleaves in nascent peptidoglycan and produces short glycan strandsJad Sassine0Manuel Pazos1Eefjan Breukink2Waldemar Vollmer3Centre for Bacterial Cell Biology, Biosciences Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, UKCentre for Bacterial Cell Biology, Biosciences Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, UKMembrane Biochemistry and Biophysics, Bijvoet Centre of Biomolecular Research, Department of Chemistry, Faculty of Science, Utrecht University, Utrecht, NetherlandsCentre for Bacterial Cell Biology, Biosciences Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, UK; Corresponding author.Bacteria encase their cytoplasmic membrane with peptidoglycan (PG) to maintain the shape of the cell and protect it from bursting. The enlargement of the PG layer is facilitated by the coordinated activities of PG synthesising and -cleaving enzymes. In Escherichia coli, the cytoplasmic membrane-bound lytic transglycosylase MltG associates with PG synthases and was suggested to terminate the polymerisation of PG glycan strands. Using pull-down and surface plasmon resonance, we detected interactions between MltG from Bacillus subtilis and two PG synthases; the class A PBP1 and the class B PBP2B. Using in vitro PG synthesis assays with radio-labelled or fluorophore-labelled B. subtilis-type and/or E. coli-type lipid II, we showed that both, BsMltG and EcMltG, are lytic tranglycosylases and that their activity is higher during ongoing glycan strand polymerisation. MltG competed with the transpeptidase activity of class A PBPs, but had no effect on their glycosyltransferase activity, and produced glycan strands with a length of 7 disaccharide units from cleavage in the nascent strands. We hypothesize that MltG cleaves the nascent strands to produce short glycan strands that are used in the cell for a yet unknown process.http://www.sciencedirect.com/science/article/pii/S2468233021000062PeptidoglycanLytic transglycosylasePenicillin-binding protein |
| spellingShingle | Jad Sassine Manuel Pazos Eefjan Breukink Waldemar Vollmer Lytic transglycosylase MltG cleaves in nascent peptidoglycan and produces short glycan strands The Cell Surface Peptidoglycan Lytic transglycosylase Penicillin-binding protein |
| title | Lytic transglycosylase MltG cleaves in nascent peptidoglycan and produces short glycan strands |
| title_full | Lytic transglycosylase MltG cleaves in nascent peptidoglycan and produces short glycan strands |
| title_fullStr | Lytic transglycosylase MltG cleaves in nascent peptidoglycan and produces short glycan strands |
| title_full_unstemmed | Lytic transglycosylase MltG cleaves in nascent peptidoglycan and produces short glycan strands |
| title_short | Lytic transglycosylase MltG cleaves in nascent peptidoglycan and produces short glycan strands |
| title_sort | lytic transglycosylase mltg cleaves in nascent peptidoglycan and produces short glycan strands |
| topic | Peptidoglycan Lytic transglycosylase Penicillin-binding protein |
| url | http://www.sciencedirect.com/science/article/pii/S2468233021000062 |
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