The outer membrane lipoprotein NlpI nucleates hydrolases within peptidoglycan multi-enzyme complexes in Escherichia coli

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Author Name

Manuel Banzhaf

Hamish C. L. Yau

Published 1 Project

Microbiology

Adam Lodge

George Kritikos

Published 1 Project

Microbiology

André Mateus

Published 1 Project

Microbiology

Ann Kristin Hov

Published 1 Project

Microbiology

Frank Stein

Published 2 Projects

Microbiology Physiology

Morgane Wartel

Published 1 Project

Microbiology

Manuel Pazos

Published 1 Project

Microbiology

Alexandra S. Solovyova

Mikhail M. Savitski

Published 1 Project

Microbiology

Athanasios Typas

Waldemar Vollmer

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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 PG synthases and hydrolases. In Escherichia coli, the activity of the two bifunctional PG synthases is driven by lipoproteins anchored in the outer membrane. However, the regulation of PG hydrolases is less well understood, with only regulators for PG amidases having been described. Here, we identify the lipoprotein NlpI as a general adaptor protein for PG hydrolases. NlpI binds to different classes of hydrolases and can specifically form multimeric complexes with various PG endopeptidases. In addition, NlpI seems to contribute both to PG elongation and cell division biosynthetic complexes based on its localization and genetic interactions. In line 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 PG regulators and adaptors are part of PG biosynthetic multi-enzyme complexes, regulating and potentially coordinating the spatiotemporal action of PG synthases and hydrolases.

Microbiology
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