ArticleNature chemical biology2021
Disorder is a critical component of lipoprotein sorting in Gram-negative bacteria.
Article in Nature chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 30 citations in OpenAlex.
- Intrinsic Disorder as a New Frontier in Antimicrobial Resistance and Bacterial Fitness.MicrobiologyOpen · 2026Review
- Article
- Structure and druggable conformation of the homodimeric lipoprotein transporter of Acinetobacter baumannii.Nature communications · 2026Article
- Identification and characterization of the functional LolB ortholog inbioRxiv : the preprint server for biology · 2026Article
- Liganded LolCDE structures reveal a common substrate-LolE interaction guiding bacterial lipoprotein transport.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Length matters: the disordered N-terminus of Pal coordinates Lpp exclusion for outer membrane constriction inJournal of bacteriology · 2026Article
- Activation of the envelope stress-responsive two-component system AmgRS compensates for depletion of the essential lipoprotein signal peptidase LspA inCurrent research in microbial sciences · 2026Article
- Peptidoglycan-outer membrane attachment generates periplasmic pressure to prevent lysis in Gram-negative bacteria.Nature microbiology · 2025Article
- A porin-like protein used by bacterial predators defines a wider lipid-trapping superfamily.Nature communications · 2025Article
- PorA of the Type IX Secretion Is a Ligand of the PorXY Two-Component Regulatory System in Porphyromonas gingivalis.Molecular microbiology · 2025Article
- Glycosylation of serine/threonine-rich intrinsically disordered regions of membrane-associated proteins in streptococci.Nature communications · 2025Article
- Deciphering the molecular basis of lipoprotein recognition and transport by LolCDE.Signal transduction and targeted therapy · 2024Article
- Heterologous protein exposure and secretion optimization in Mycoplasma pneumoniae.Microbial cell factories · 2024Article
- ACAD10 and ACAD11 allow entry of 4-hydroxy fatty acids into β-oxidation.Cellular and molecular life sciences : CMLS · 2024Article
- Lipoprotein transport system Lol may be a selective target for Gram-negative bacteria.Frontiers in cellular and infection microbiology · 2024Article
- Altering Escherichia coli envelope integrity by mimicking the lipoprotein RcsF.Archives of microbiology · 2023Article
- Identification of an Essential LolD-Like Protein in Helicobacter pylori.Journal of bacteriology · 2023Article
- Sensitive and selective polymer condensation at membrane surface driven by positive co-operativity.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Envelope-Stress Sensing Mechanism of Rcs and Cpx Signaling Pathways in Gram-Negative Bacteria.Journal of microbiology (Seoul, Korea) · 2023Review
- Conformational rearrangements in the sensory RcsF/OMP complex mediate signal transduction across the bacterial cell envelope.PLoS genetics · 2023Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gram-negative bacteria express structurally diverse lipoproteins in their cell envelope. Here, we find that approximately half of lipoproteins destined to the Escherichia coli outer membrane display an intrinsically disordered linker at their N terminus. Intrinsically disordered regions are common in proteins, but establishing their importance in vivo has remained challenging. As we sought to unravel how lipoproteins mature, we discovered that unstructured linkers are required for optimal trafficking by the Lol lipoprotein sorting system, whereby linker deletion re-routes three unrelated lipoproteins to the inner membrane. Focusing on the stress sensor RcsF, we found that replacing the linker with an artificial peptide restored normal outer-membrane targeting only when the peptide was of similar length and disordered. Overall, this study reveals the role played by intrinsic disorder in lipoprotein sorting, providing mechanistic insight into the biogenesis of these proteins and suggesting that evolution can select for intrinsic disorder that supports protein function.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.