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Outer membrane lipoprotein NlpI scaffolds peptidoglycan hydrolases within multi‐enzyme complexes in Escherichia coli
Author(s) -
Banzhaf Manuel,
Yau Hamish CL,
Verheul Jolanda,
Lodge Adam,
Kritikos George,
Mateus André,
Cordier Baptiste,
Hov Ann Kristin,
Stein Frank,
Wartel Morgane,
Pazos Manuel,
Solovyova Alexandra S,
Breukink Eefjan,
van Teeffelen Sven,
Savitski Mikhail M,
den Blaauwen Tanneke,
Typas Athanasios,
Vollmer Waldemar
Publication year - 2020
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.15252/embj.2019102246
Subject(s) - biology , escherichia coli , peptidoglycan , bacterial outer membrane , enzyme , biochemistry , microbiology and biotechnology , escherichia coli proteins , gene
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.