Outer membrane lipoprotein NlpI scaffolds peptidoglycan hydrolases within multi-enzyme complexes in Escherichia coli
Research output: Contribution to journal › Article › peer-review
Colleges, School and Institutes
- European Molecular Biology Laboratory, Genome Biology Unit, 69117 Heidelberg, Germany.
- Newcastle University
- University of Amsterdam
- Microbial Morphogenesis and Growth Lab, Institut Pasteur, Paris, France.
- Newcastle University Protein and Proteome Analysis, Newcastle Upon Tyne, UK.
- Membrane Biochemistry and Biophysics, Department of Chemistry, Faculty of Science, Utrecht University, Utrecht, The Netherlands.
- European Molecular Biology Laboratory, Structural & Computational Biology Unit, Heidelberg, Germany. email@example.com.
- European Molecular Biology Laboratory Heidelberg, Genome Biology Unit, Meyerhofstraße 1, 69117, Heidelberg, Germany.
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.
|Number of pages||20|
|Journal||The EMBO journal|
|Early online date||3 Feb 2020|
|Publication status||Published - 2 Mar 2020|