Outer membrane lipoprotein NlpI scaffolds peptidoglycan hydrolases within multi‐enzyme complexes in Escherichia coli
The peptidoglycan (PG) sacculus provides bacteria with the mechanical strength to maintain cell shape and resist osmotic stress. Enlargement of the mesh‐like sacculus requires the combined activity of peptidoglycan synthases and hydrolases. In Escherichia coli , the activity of two PG synthases is d...
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| Published in | The EMBO journal Vol. 39; no. 5; pp. e102246 - n/a |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing Group UK
02.03.2020
Springer Nature B.V EMBO Press John Wiley and Sons Inc |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0261-4189 1460-2075 1460-2075 |
| DOI | 10.15252/embj.2019102246 |
Cover
| Abstract | The peptidoglycan (PG) sacculus provides bacteria with the mechanical strength to maintain cell shape and resist osmotic stress. Enlargement of the mesh‐like sacculus requires the combined activity of peptidoglycan synthases and hydrolases. In
Escherichia coli
, the activity of two PG synthases is driven by lipoproteins anchored in the outer membrane (OM). However, the regulation of PG hydrolases is less well understood, with only regulators for PG amidases having been described. Here, we identify the OM lipoprotein NlpI as a general adaptor protein for PG hydrolases. NlpI binds to different classes of hydrolases and can specifically form complexes with various PG endopeptidases. In addition, NlpI seems to contribute both to PG elongation and division biosynthetic complexes based on its localization and genetic interactions. Consistent with such a role, we reconstitute PG multi‐enzyme complexes containing NlpI, the PG synthesis regulator LpoA, its cognate bifunctional synthase, PBP1A, and different endopeptidases. Our results indicate that peptidoglycan regulators and adaptors are part of PG biosynthetic multi‐enzyme complexes, regulating and potentially coordinating the spatiotemporal action of PG synthases and hydrolases.
Synopsis
In bacteria, enzyme activities regulating peptidoglycan biosynthesis and degradation have to be adjusted during cell wall growth. Here, the outer membrane‐anchored lipoprotein NlpI is shown to facilitate formation of peptidoglycan synthase and hydrolase multi‐enzyme complexes to coordinate correct enlargement of the cell wall peptidoglycan layer in
E. coli
.
NlpI binds to different classes of peptidoglycan hydrolases.
NlpI can specifically form multimeric complexes with various endopeptidases.
NlpI contributes to peptidoglycan biosynthetic complexes active in cell elongation and cell division based on its cellular localization and genetic interactions.
NlpI forms multi‐enzyme complexes containing peptidoglycan synthases and hydrolases
in vitro
.
Graphical Abstract
An adaptor protein for peptidoglycan hydrolases and synthases coordinates bacterial cell wall growth. |
|---|---|
| AbstractList | The peptidoglycan (PG) sacculus provides bacteria with the mechanical strength to maintain cell shape and resist osmotic stress. Enlargement of the mesh‐like sacculus requires the combined activity of peptidoglycan synthases and hydrolases. In Escherichia coli, the activity of two PG synthases is driven by lipoproteins anchored in the outer membrane (OM). However, the regulation of PG hydrolases is less well understood, with only regulators for PG amidases having been described. Here, we identify the OM lipoprotein NlpI as a general adaptor protein for PG hydrolases. NlpI binds to different classes of hydrolases and can specifically form complexes with various PG endopeptidases. In addition, NlpI seems to contribute both to PG elongation and division biosynthetic complexes based on its localization and genetic interactions. Consistent with such a role, we reconstitute PG multi‐enzyme complexes containing NlpI, the PG synthesis regulator LpoA, its cognate bifunctional synthase, PBP1A, and different endopeptidases. Our results indicate that peptidoglycan regulators and adaptors are part of PG biosynthetic multi‐enzyme complexes, regulating and potentially coordinating the spatiotemporal action of PG synthases and hydrolases.
Synopsis
In bacteria, enzyme activities regulating peptidoglycan biosynthesis and degradation have to be adjusted during cell wall growth. Here, the outer membrane‐anchored lipoprotein NlpI is shown to facilitate formation of peptidoglycan synthase and hydrolase multi‐enzyme complexes to coordinate correct enlargement of the cell wall peptidoglycan layer in E. coli.
NlpI binds to different classes of peptidoglycan hydrolases.
NlpI can specifically form multimeric complexes with various endopeptidases.
NlpI contributes to peptidoglycan biosynthetic complexes active in cell elongation and cell division based on its cellular localization and genetic interactions.
NlpI forms multi‐enzyme complexes containing peptidoglycan synthases and hydrolases in vitro.
An adaptor protein for peptidoglycan hydrolases and synthases coordinates bacterial cell wall growth. The peptidoglycan ( PG ) sacculus provides bacteria with the mechanical strength to maintain cell shape and resist osmotic stress. Enlargement of the mesh‐like sacculus requires the combined activity of peptidoglycan synthases and hydrolases. In Escherichia coli , the activity of two PG synthases is driven by lipoproteins anchored in the outer membrane ( OM ). However, the regulation of PG hydrolases is less well understood, with only regulators for PG amidases having been described. Here, we identify the OM lipoprotein NlpI as a general adaptor protein for PG hydrolases. NlpI binds to different classes of hydrolases and can specifically form complexes with various PG endopeptidases. In addition, NlpI seems to contribute both to PG elongation and division biosynthetic complexes based on its localization and genetic interactions. Consistent with such a role, we reconstitute PG multi‐enzyme complexes containing NlpI, the PG synthesis regulator LpoA, its cognate bifunctional synthase, PBP 1A, and different endopeptidases. Our results indicate that peptidoglycan regulators and adaptors are part of PG biosynthetic multi‐enzyme complexes, regulating and potentially coordinating the spatiotemporal action of PG synthases and hydrolases. An adaptor protein for peptidoglycan hydrolases and synthases coordinates bacterial cell wall growth. The peptidoglycan (PG) sacculus provides bacteria with the mechanical strength to maintain cell shape and resist osmotic stress. Enlargement of the mesh-like sacculus requires the combined activity of peptidoglycan synthases and hydrolases. In Escherichia coli, the activity of two PG synthases is driven by lipoproteins anchored in the outer membrane (OM). However, the regulation of PG hydrolases is less well understood, with only regulators for PG amidases having been described. Here, we identify the OM lipoprotein NlpI as a general adaptor protein for PG hydrolases. NlpI binds to different classes of hydrolases and can specifically form complexes with various PG endopeptidases. In addition, NlpI seems to contribute both to PG elongation and division biosynthetic complexes based on its localization and genetic interactions. Consistent with such a role, we reconstitute PG multi-enzyme complexes containing NlpI, the PG synthesis regulator LpoA, its cognate bifunctional synthase, PBP1A, and different endopeptidases. Our results indicate that peptidoglycan regulators and adaptors are part of PG biosynthetic multi-enzyme complexes, regulating and potentially coordinating the spatiotemporal action of PG synthases and hydrolases. The peptidoglycan (PG) sacculus provides bacteria with the mechanical strength to maintain cell shape and resist osmotic stress. Enlargement of the mesh-like sacculus requires the combined activity of peptidoglycan synthases and hydrolases. In Escherichia coli, the activity of two PG synthases is driven by lipoproteins anchored in the outer membrane (OM). However, the regulation of PG hydrolases is less well understood, with only regulators for PG amidases having been described. Here, we identify the OM lipoprotein NlpI as a general adaptor protein for PG hydrolases. NlpI binds to different classes of hydrolases and can specifically form complexes with various PG endopeptidases. In addition, NlpI seems to contribute both to PG elongation and division biosynthetic complexes based on its localization and genetic interactions. Consistent with such a role, we reconstitute PG multi-enzyme complexes containing NlpI, the PG synthesis regulator LpoA, its cognate bifunctional synthase, PBP1A, and different endopeptidases. Our results indicate that peptidoglycan regulators and adaptors are part of PG biosynthetic multi-enzyme complexes, regulating and potentially coordinating the spatiotemporal action of PG synthases and hydrolases.The peptidoglycan (PG) sacculus provides bacteria with the mechanical strength to maintain cell shape and resist osmotic stress. Enlargement of the mesh-like sacculus requires the combined activity of peptidoglycan synthases and hydrolases. In Escherichia coli, the activity of two PG synthases is driven by lipoproteins anchored in the outer membrane (OM). However, the regulation of PG hydrolases is less well understood, with only regulators for PG amidases having been described. Here, we identify the OM lipoprotein NlpI as a general adaptor protein for PG hydrolases. NlpI binds to different classes of hydrolases and can specifically form complexes with various PG endopeptidases. In addition, NlpI seems to contribute both to PG elongation and division biosynthetic complexes based on its localization and genetic interactions. Consistent with such a role, we reconstitute PG multi-enzyme complexes containing NlpI, the PG synthesis regulator LpoA, its cognate bifunctional synthase, PBP1A, and different endopeptidases. Our results indicate that peptidoglycan regulators and adaptors are part of PG biosynthetic multi-enzyme complexes, regulating and potentially coordinating the spatiotemporal action of PG synthases and hydrolases. The peptidoglycan (PG) sacculus provides bacteria with the mechanical strength to maintain cell shape and resist osmotic stress. Enlargement of the mesh-like sacculus requires the combined activity of peptidoglycan synthases and hydrolases. In Escherichia coli, the activity of two PG synthases is driven by lipoproteins anchored in the outer membrane (OM). However, the regulation of PG hydrolases is less well understood, with only regulators for PG amidases having been described. Here, we identify the OM lipoprotein NlpI as a general adaptor protein for PG hydro-lases. NlpI binds to different classes of hydrolases and can specifically form complexes with various PG endopeptidases. In addition, NlpI seems to contribute both to PG elongation and division biosynthetic complexes based on its localization and genetic interactions. Consistent with such a role, we reconstitute PG multi-enzyme complexes containing NlpI, the PG synthesis regulator LpoA, its cognate bifunctional synthase, PBP1A, and different endopeptidases. Our results indicate that peptidoglycan regulators and adaptors are part of PG biosynthetic multi-enzyme complexes, regulating and potentially coordinating the spatiotemporal action of PG synthases and hydrolases. The peptidoglycan (PG) sacculus provides bacteria with the mechanical strength to maintain cell shape and resist osmotic stress. Enlargement of the mesh‐like sacculus requires the combined activity of peptidoglycan synthases and hydrolases. In Escherichia coli , the activity of two PG synthases is driven by lipoproteins anchored in the outer membrane (OM). However, the regulation of PG hydrolases is less well understood, with only regulators for PG amidases having been described. Here, we identify the OM lipoprotein NlpI as a general adaptor protein for PG hydrolases. NlpI binds to different classes of hydrolases and can specifically form complexes with various PG endopeptidases. In addition, NlpI seems to contribute both to PG elongation and division biosynthetic complexes based on its localization and genetic interactions. Consistent with such a role, we reconstitute PG multi‐enzyme complexes containing NlpI, the PG synthesis regulator LpoA, its cognate bifunctional synthase, PBP1A, and different endopeptidases. Our results indicate that peptidoglycan regulators and adaptors are part of PG biosynthetic multi‐enzyme complexes, regulating and potentially coordinating the spatiotemporal action of PG synthases and hydrolases. Synopsis In bacteria, enzyme activities regulating peptidoglycan biosynthesis and degradation have to be adjusted during cell wall growth. Here, the outer membrane‐anchored lipoprotein NlpI is shown to facilitate formation of peptidoglycan synthase and hydrolase multi‐enzyme complexes to coordinate correct enlargement of the cell wall peptidoglycan layer in E. coli . NlpI binds to different classes of peptidoglycan hydrolases. NlpI can specifically form multimeric complexes with various endopeptidases. NlpI contributes to peptidoglycan biosynthetic complexes active in cell elongation and cell division based on its cellular localization and genetic interactions. NlpI forms multi‐enzyme complexes containing peptidoglycan synthases and hydrolases in vitro . Graphical Abstract An adaptor protein for peptidoglycan hydrolases and synthases coordinates bacterial cell wall growth. |
| Author | Verheul, Jolanda Mateus, André Hov, Ann Kristin Breukink, Eefjan Banzhaf, Manuel Vollmer, Waldemar Cordier, Baptiste Yau, Hamish CL Wartel, Morgane Solovyova, Alexandra S Kritikos, George Stein, Frank van Teeffelen, Sven Typas, Athanasios Lodge, Adam Pazos, Manuel Savitski, Mikhail M den Blaauwen, Tanneke |
| AuthorAffiliation | 6 Membrane Biochemistry and Biophysics Department of Chemistry Faculty of Science Utrecht University Utrecht The Netherlands 4 Microbial Morphogenesis and Growth Lab Institut Pasteur Paris France 1 European Molecular Biology Laboratory Genome Biology Unit Heidelberg Germany 3 Bacterial Cell Biology & Physiology Swammerdam Institute for Life Sciences Faculty of Science University of Amsterdam Amsterdam The Netherlands 5 Newcastle University Protein and Proteome Analysis Newcastle Upon Tyne UK 10 Present address: Iksuda Therapeutics The Biosphere Newcastle Upon Tyne UK 8 Present address: Institute of Microbiology & Infection and School of Biosciences University of Birmingham Edgbaston Birmingham UK 11 Present address: École polytechnique fédérale de Lausanne SV IBI‐SV UPDALPE, AAB 013 Lausanne Switzerland 9 Present address: Faculty of Science, Agriculture and Engineering Newcastle University Newcastle Upon Tyne UK 7 European Molecular Biology Laboratory Structural & Computational Unit Heidelberg |
| AuthorAffiliation_xml | – name: 1 European Molecular Biology Laboratory Genome Biology Unit Heidelberg Germany – name: 2 Centre for Bacterial Cell Biology Biosciences Institute Newcastle University Newcastle Upon Tyne UK – name: 5 Newcastle University Protein and Proteome Analysis Newcastle Upon Tyne UK – name: 7 European Molecular Biology Laboratory Structural & Computational Unit Heidelberg Germany – name: 6 Membrane Biochemistry and Biophysics Department of Chemistry Faculty of Science Utrecht University Utrecht The Netherlands – name: 8 Present address: Institute of Microbiology & Infection and School of Biosciences University of Birmingham Edgbaston Birmingham UK – name: 9 Present address: Faculty of Science, Agriculture and Engineering Newcastle University Newcastle Upon Tyne UK – name: 3 Bacterial Cell Biology & Physiology Swammerdam Institute for Life Sciences Faculty of Science University of Amsterdam Amsterdam The Netherlands – name: 11 Present address: École polytechnique fédérale de Lausanne SV IBI‐SV UPDALPE, AAB 013 Lausanne Switzerland – name: 4 Microbial Morphogenesis and Growth Lab Institut Pasteur Paris France – name: 10 Present address: Iksuda Therapeutics The Biosphere Newcastle Upon Tyne UK |
| Author_xml | – sequence: 1 givenname: Manuel surname: Banzhaf fullname: Banzhaf, Manuel organization: European Molecular Biology Laboratory, Genome Biology Unit, Institute of Microbiology & Infection and School of Biosciences, University of Birmingham – sequence: 2 givenname: Hamish CL surname: Yau fullname: Yau, Hamish CL organization: Centre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Faculty of Science, Agriculture and Engineering, Newcastle University – sequence: 3 givenname: Jolanda surname: Verheul fullname: Verheul, Jolanda organization: Bacterial Cell Biology & Physiology, Swammerdam Institute for Life Sciences, Faculty of Science, University of Amsterdam – sequence: 4 givenname: Adam surname: Lodge fullname: Lodge, Adam organization: Centre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Iksuda Therapeutics, The Biosphere – sequence: 5 givenname: George surname: Kritikos fullname: Kritikos, George organization: European Molecular Biology Laboratory, Genome Biology Unit – sequence: 6 givenname: André orcidid: 0000-0001-6870-0677 surname: Mateus fullname: Mateus, André organization: European Molecular Biology Laboratory, Genome Biology Unit – sequence: 7 givenname: Baptiste orcidid: 0000-0002-6042-9787 surname: Cordier fullname: Cordier, Baptiste organization: Microbial Morphogenesis and Growth Lab, Institut Pasteur – sequence: 8 givenname: Ann Kristin surname: Hov fullname: Hov, Ann Kristin organization: European Molecular Biology Laboratory, Genome Biology Unit, École polytechnique fédérale de Lausanne SV IBI‐SV UPDALPE, AAB 013 – sequence: 9 givenname: Frank surname: Stein fullname: Stein, Frank organization: European Molecular Biology Laboratory, Genome Biology Unit – sequence: 10 givenname: Morgane surname: Wartel fullname: Wartel, Morgane organization: European Molecular Biology Laboratory, Genome Biology Unit – sequence: 11 givenname: Manuel surname: Pazos fullname: Pazos, Manuel organization: Centre for Bacterial Cell Biology, Biosciences Institute, Newcastle University – sequence: 12 givenname: Alexandra S surname: Solovyova fullname: Solovyova, Alexandra S organization: Newcastle University Protein and Proteome Analysis – sequence: 13 givenname: Eefjan surname: Breukink fullname: Breukink, Eefjan organization: Membrane Biochemistry and Biophysics, Department of Chemistry, Faculty of Science, Utrecht University – sequence: 14 givenname: Sven surname: van Teeffelen fullname: van Teeffelen, Sven organization: Microbial Morphogenesis and Growth Lab, Institut Pasteur – sequence: 15 givenname: Mikhail M orcidid: 0000-0003-2011-9247 surname: Savitski fullname: Savitski, Mikhail M organization: European Molecular Biology Laboratory, Genome Biology Unit, European Molecular Biology Laboratory, Structural & Computational Unit – sequence: 16 givenname: Tanneke orcidid: 0000-0002-5403-5597 surname: den Blaauwen fullname: den Blaauwen, Tanneke email: t.denblaauwen@uva.nl organization: Bacterial Cell Biology & Physiology, Swammerdam Institute for Life Sciences, Faculty of Science, University of Amsterdam – sequence: 17 givenname: Athanasios orcidid: 0000-0002-0797-9018 surname: Typas fullname: Typas, Athanasios email: typas@embl.de organization: European Molecular Biology Laboratory, Genome Biology Unit, European Molecular Biology Laboratory, Structural & Computational Unit – sequence: 18 givenname: Waldemar orcidid: 0000-0003-0408-8567 surname: Vollmer fullname: Vollmer, Waldemar email: w.vollmer@ncl.ac.uk organization: Centre for Bacterial Cell Biology, Biosciences Institute, Newcastle University |
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| Issue | 5 |
| Keywords | peptidoglycan bacterial cell envelope endopeptidase outer membrane lipoprotein penicillin‐binding protein penicillin-binding protein Virology & Host Pathogen Interaction outer membrane lipopro- tein peptidoglycan Subject Category Microbiology |
| Language | English |
| License | Attribution 2020 The Authors. Published under the terms of the CC BY 4.0 license. Attribution: http://creativecommons.org/licenses/by This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
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| Snippet | The peptidoglycan (PG) sacculus provides bacteria with the mechanical strength to maintain cell shape and resist osmotic stress. Enlargement of the mesh‐like... The peptidoglycan (PG) sacculus provides bacteria with the mechanical strength to maintain cell shape and resist osmotic stress. Enlargement of the mesh-like... The peptidoglycan ( PG ) sacculus provides bacteria with the mechanical strength to maintain cell shape and resist osmotic stress. Enlargement of the mesh‐like... |
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| SubjectTerms | Adapters Antibiotics Bacteria bacterial cell envelope Biochemistry Biochemistry, Molecular Biology Biodegradation Biosynthesis Cell division Cell size Cell Wall - enzymology Cell walls E coli Elongation EMBO23 endopeptidase Endopeptidases - genetics Endopeptidases - metabolism Enlargement Enzymatic activity Enzymes Escherichia coli Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Hydrolase Life Sciences Lipoproteins Lipoproteins - genetics Lipoproteins - metabolism Localization Mechanical properties Membranes Multienzyme Complexes N-Acetylmuramoyl-L-alanine Amidase - genetics N-Acetylmuramoyl-L-alanine Amidase - metabolism Osmotic stress outer membrane lipoprotein Penicillin penicillin‐binding protein peptidoglycan Peptidoglycan - metabolism Peptidoglycans Regulators Saccule |
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| Title | Outer membrane lipoprotein NlpI scaffolds peptidoglycan hydrolases within multi‐enzyme complexes in Escherichia coli |
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