Outer membrane lipoprotein NlpI scaffolds peptidoglycan hydrolases within multi-enzyme complexes in Escherichia coli

被引：62

作者：

Banzhaf, Manuel ^{[1
,8
,9
]}

Yau, Hamish C. L. ^{[2
,10
]}

Verheul, Jolanda ^{[3
]}

Lodge, Adam ^{[2
,11
]}

Kritikos, George ^{[1
]}

Mateus, Andre ^{[1
]}

Cordier, Baptiste ^{[4
]}

Hov, Ann Kristin ^{[1
,12
]}

Stein, Frank ^{[1
]}

Wartel, Morgane ^{[1
]}

Pazos, Manuel ^{[2
]}

Solovyova, Alexandra S. ^{[5
]}

Breukink, Eefjan ^{[6
]}

van Teeffelen, Sven ^{[4
]}

Savitski, Mikhail M. ^{[1
,7
]}

den Blaauwen, Tanneke ^{[3
]}

Typas, Athanasios ^{[1
,7
]}

Vollmer, Waldemar ^{[2
]}

机构：

[1] European Mol Biol Lab, Genome Biol Unit, Heidelberg, Germany

[2] Newcastle Univ, Ctr Bacterial Cell Biol, Biosci Inst, Newcastle Upon Tyne, Tyne & Wear, England

[3] Univ Amsterdam, Fac Sci, Swammerdam Inst Life Sci, Bacterial Cell Biol & Physiol, Amsterdam, Netherlands

[4] Inst Pasteur, Microbial Morphogenesis & Growth Lab, Paris, France

[5] Newcastle Univ Prot & Proteome Anal, Newcastle Upon Tyne, Tyne & Wear, England

[6] Univ Utrecht, Fac Sci, Dept Chem, Membrane Biochem & Biophys, Utrecht, Netherlands

[7] European Mol Biol Lab, Struct & Computat Unit, Heidelberg, Germany

[8] Univ Birmingham, Inst Microbiol & Infect, Birmingham, W Midlands, England

[9] Univ Birmingham, Sch Biosci, Birmingham, W Midlands, England

[10] Newcastle Univ, Fac Sci Agr & Engn, Newcastle Upon Tyne, Tyne & Wear, England

[11] Iksuda Therapeut, Biosphere, Newcastle Upon Tyne, Tyne & Wear, England

[12] Ecole Polytech Fed Lausanne, SV IBI SV UPDALPE, AAB 013, Lausanne, Switzerland

来源：

EMBO JOURNAL | 2020年 / 39卷 / 05期

基金：

英国惠康基金; 英国医学研究理事会; 欧洲研究理事会;

关键词：

bacterial cell envelope; endopeptidase; outer membrane lipoprotein; penicillin-binding protein; peptidoglycan; DAUGHTER CELL-SEPARATION; TETRATRICOPEPTIDE REPEAT; CRYSTAL-STRUCTURE; LYTM-DOMAIN; PROTEIN; WALL; IDENTIFICATION; MUREIN; BINDING; ACTIVATOR;

D O I：

10.15252/embj.2019102246

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

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.

引用

页数：20

共 76 条

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