ArticleThe Journal of biological chemistry2011
Outer membrane targeting of secretin PulD protein relies on disordered domain recognition by a dedicated chaperone.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 37 citations in OpenAlex.
- Structural characterization and functional insights into the type II secretion system of the poly-extremophile Deinococcus radiodurans.The Journal of biological chemistry · 2024Article
- Protein intrinsic viscosity determination with the Viscosizer TD instrument: reaching beyond the initially expected applications.European biophysics journal : EBJ · 2021Article
- Bacterial secretins: Mechanisms of assembly and membrane targeting.Protein science : a publication of the Protein Society · 2020Review
- Yeast can express and assemble bacterial secretins in the mitochondrial outer membrane.Microbial cell (Graz, Austria) · 2019Article
- Structure and assembly of pilotin-dependent and -independent secretins of the type II secretion system.PLoS pathogens · 2019Article
- Structural insight into the assembly of the type II secretion system pilotin-secretin complex from enterotoxigenic Escherichia coli.Nature microbiology · 2018Article
- Structure and Membrane Topography of the Vibrio-Type Secretin Complex from the Type 2 Secretion System of Enteropathogenic Escherichia coli.Journal of bacteriology · 2018Article
- Article
- Structural insights into the secretin translocation channel in the type II secretion system.Nature structural & molecular biology · 2017Article
- Prepore Stability Controls Productive Folding of the BAM-independent Multimeric Outer Membrane Secretin PulD.The Journal of biological chemistry · 2017Article
- Lipids assist the membrane insertion of a BAM-independent outer membrane protein.Scientific reports · 2015Article
- Secretion of bacterial lipoproteins: through the cytoplasmic membrane, the periplasm and beyond.Biochimica et biophysica acta · 2014Review
- Bacterial secretins form constitutively open pores akin to general porins.Journal of bacteriology · 2014Article
- Sequential steps in the assembly of the multimeric outer membrane secretin PulD.The Journal of biological chemistry · 2013Article
- Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS.PLoS pathogens · 2013Article
- A Single Amino Acid Substitution Changes the Self-Assembly Status of a Type IV Piliation Secretin.Journal of bacteriology · 2012Article
- On the path to uncover the bacterial type II secretion system.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- The type II secretion system: biogenesis, molecular architecture and mechanism.Nature reviews. Microbiology · 2012Review
- Structural insights into the Type II secretion nanomachine.Current opinion in structural biology · 2012Review
- Outer membrane targeting, ultrastructure, and single molecule localization of the enteropathogenic Escherichia coli type IV pilus secretin BfpB.Journal of bacteriology · 2012Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Interaction of bacterial outer membrane secretin PulD with its dedicated lipoprotein chaperone PulS relies on a disorder-to-order transition of the chaperone binding (S) domain near the PulD C terminus. PulS interacts with purified S domain to form a 1:1 complex. Circular dichroism, one-dimensional NMR, and hydrodynamic measurements indicate that the S domain is elongated and intrinsically disordered but gains secondary structure upon binding to PulS. Limited proteolysis and mass spectrometry identified the 28 C-terminal residues of the S domain as a minimal binding site with low nanomolar affinity for PulS in vitro that is sufficient for outer membrane targeting of PulD in vivo. The region upstream of this binding site is not required for targeting or multimerization and does not interact with PulS, but it is required for secretin function in type II secretion. Although other secretin chaperones differ substantially from PulS in sequence and secondary structure, they have all adopted at least superficially similar mechanisms of interaction with their cognate secretins, suggesting that intrinsically disordered regions facilitate rapid interaction between secretins and their chaperones.
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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.