Reference - Detail
| RRC ID | 59090 |
|---|---|
| Author | Banzhaf M, Yau HC, Verheul J, Lodge A, Kritikos G, Mateus A, Cordier B, Hov AK, Stein F, Wartel M, Pazos M, Solovyova AS, Breukink E, van Teeffelen S, Savitski MM, den Blaauwen T, Typas A, Vollmer W. |
| Title | Outer membrane lipoprotein NlpI scaffolds peptidoglycan hydrolases within multi-enzyme complexes in Escherichia coli. |
| Journal | EMBO J |
| 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. |
| Volume | 39(5) |
| Pages | e102246 |
| Published | 2020-3-2 |
| DOI | 10.15252/embj.2019102246 |
| PMID | 32009249 |
| PMC | PMC7049810 |
| MeSH | Cell Wall / enzymology Endopeptidases / genetics Endopeptidases / metabolism Escherichia coli / enzymology* Escherichia coli / genetics Escherichia coli Proteins / genetics Escherichia coli Proteins / metabolism* Lipoproteins / genetics Lipoproteins / metabolism* Multienzyme Complexes* N-Acetylmuramoyl-L-alanine Amidase / genetics N-Acetylmuramoyl-L-alanine Amidase / metabolism* Peptidoglycan / metabolism |
| IF | 11.227 |
| Times Cited | 4 |
| Altmetric score |
オルトメトリクス指標項目
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| The most frequently cited source | X(Twitter) |
| Total number of mentions | 28 |
| Altmetric score changes over past 6months | 0.0 |
| Resource | |
| Prokaryotes E. coli | Keio collection ASKA library |