ArticleThe Journal of biological chemistry2011
The Chlamydia effector chlamydial outer protein N (CopN) sequesters tubulin and prevents microtubule assembly.
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 32 papers.
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Who cites it
32 citing papers in PubMed, 47 citations in OpenAlex.
- Insights into the association of the Chlamydia trachomatis type III secretion chaperone complex, Scc4:Scc1, from sequential expression in Escherichia coli.Protein expression and purification · 2024Article
- BopN is a Gatekeeper of theMicrobiology spectrum · 2023Article
- A Functional Yeast-Based Screen Identifies the Host Microtubule Cytoskeleton as a Target of NumerousInternational journal of molecular sciences · 2023Article
- Molecular pathogenesis ofFrontiers in cellular and infection microbiology · 2023Review
- Ecology and evolution of chlamydial symbionts of arthropods.ISME communications · 2022Article
- Pangenomics reveals alternative environmental lifestyles among chlamydiae.Nature communications · 2021Article
- Robust Heat Shock Response inFrontiers in microbiology · 2021Article
- Chain-Selective Isotopic Labeling of the Heterodimeric Type III Secretion Chaperone, Scc4:Scc1, Reveals the Total Structural Rearrangement of theBiomolecules · 2020Article
- Review
- Identification of specific sequence motif of YopN of Yersinia pseudotuberculosis required for systemic infection.Virulence · 2019Article
- Purification of Tag-FreeBiochemistry · 2019Article
- The multiple functions of the numerousMicrobial cell (Graz, Austria) · 2019Review
- Insight into microtubule nucleation from tubulin-capping proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Stathmin recruits tubulin to Listeria monocytogenes-induced actin comets and promotes bacterial dissemination.Cellular and molecular life sciences : CMLS · 2019Article
- YopN Is Required for Efficient Effector Translocation and Virulence in Yersinia pseudotuberculosis.Infection and immunity · 2018Article
- Evolutionary Genetics of Cytoplasmic Incompatibility Genes cifA and cifB in Prophage WO of Wolbachia.Genome biology and evolution · 2018Article
- Steps for Shigella Gatekeeper Protein MxiC Function in Hierarchical Type III Secretion Regulation.The Journal of biological chemistry · 2017Article
- A working model for the type III secretion mechanism in Chlamydia.Microbes and infection · 2016Review
- Multipart Chaperone-Effector Recognition in the Type III Secretion System of Chlamydia trachomatis.The Journal of biological chemistry · 2015Article
- Chlamydia trachomatis Type III Secretion Proteins Regulate Transcription.Journal of bacteriology · 2015Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Chlamydia species are obligate intracellular pathogens that utilize a type three secretion system to manipulate host cell processes. Genetic manipulations are currently not possible in Chlamydia, necessitating study of effector proteins in heterologous expression systems and severely complicating efforts to relate molecular strategies used by Chlamydia to the biochemical activities of effector proteins. CopN is a chlamydial type three secretion effector that is essential for virulence. Heterologous expression of CopN in cells results in loss of microtubule spindles and metaphase plate formation and causes mitotic arrest. CopN is a multidomain protein with similarity to type three secretion system "plug" proteins from other organisms but has functionally diverged such that it also functions as an effector protein. We show that CopN binds directly to αβ-tubulin but not to microtubules (MTs). Furthermore, CopN inhibits tubulin polymerization by sequestering free αβ-tubulin, similar to one of the mechanisms utilized by stathmin. Although CopN and stathmin share no detectable sequence identity, both influence MT formation by sequestration of αβ-tubulin. CopN displaces stathmin from preformed stathmin-tubulin complexes, indicating that the proteins bind overlapping sites on tubulin. CopN is the first bacterial effector shown to disrupt MT formation directly. This recognition affords a mechanistic understanding of a strategy Chlamydia species use to manipulate the host cell cycle.
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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.