ArticleThe Journal of biological chemistry2012
The Salmonella type III secretion system inner rod protein PrgJ is partially folded.
Article in The Journal of biological chemistry, 2012. 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, 33 citations in OpenAlex.
- The Co-Evolutionary Arms Race BetweenMicroorganisms · 2026Review
- Article
- Type three secretion system in Salmonella Typhimurium: the key to infection.Genes & genomics · 2020Review
- T3S injectisome needle complex structures in four distinct states reveal the basis of membrane coupling and assembly.Nature microbiology · 2019Article
- On the road to structure-based development of anti-virulence therapeutics targeting the type III secretion system injectisome.MedChemComm · 2019Review
- The Injectisome, a Complex Nanomachine for Protein Injection into Mammalian Cells.EcoSal Plus · 2019Review
- A protein secreted by theeLife · 2018Article
- The inner-rod component of Shigella flexneri type 3 secretion system, MxiI, is involved in the transmission of the secretion activation signal by its interaction with MxiC.MicrobiologyOpen · 2018Article
- Characterization of the Ruler Protein Interaction Interface on the Substrate Specificity Switch Protein in theThe Journal of biological chemistry · 2017Article
- The Structure and Function of Type III Secretion Systems.Microbiology spectrum · 2016Review
- Nuclear Magnetic Resonance Characterization of the Type III Secretion System Tip Chaperone Protein PcrG of Pseudomonas aeruginosa.Biochemistry · 2015Article
- The LcrG Tip Chaperone Protein of the Yersinia pestis Type III Secretion System Is Partially Folded.Journal of molecular biology · 2015Article
- Structural analysis of a specialized type III secretion system peptidoglycan-cleaving enzyme.The Journal of biological chemistry · 2015Article
- Salmonellae interactions with host processes.Nature reviews. Microbiology · 2015Review
- NMR model of PrgI-SipD interaction and its implications in the needle-tip assembly of the Salmonella type III secretion system.Journal of molecular biology · 2014Article
- Building a secreting nanomachine: a structural overview of the T3SS.Current opinion in structural biology · 2014Review
- Caspase-1-dependent and -independent cell death pathways in Burkholderia pseudomallei infection of macrophages.PLoS pathogens · 2014Article
- The inner rod protein controls substrate switching and needle length in a Salmonella type III secretion system.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Bacterial type III secretion systems: specialized nanomachines for protein delivery into target cells.Annual review of microbiology · 2014Review
- Structure and biophysics of type III secretion in bacteria.Biochemistry · 2013Review
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
The type III secretion system (T3SS) is essential in the pathogenesis of many bacteria. The inner rod is important in the assembly of the T3SS needle complex. However, the atomic structure of the inner rod protein is currently unknown. Based on computational methods, others have suggested that the Salmonella inner rod protein PrgJ is highly helical, forming a folded 3 helix structure. Here we show by CD and NMR spectroscopy that the monomeric form of PrgJ lacks a tertiary structure, and the only well-structured part of PrgJ is a short α-helix at the C-terminal region from residues 65-82. Disruption of this helix by glycine or proline mutation resulted in defective assembly of the needle complex, rendering bacteria incapable of secreting effector proteins. Likewise, CD and NMR data for the Shigella inner rod protein MxiI indicate this protein lacks a tertiary structure as well. Our results reveal that the monomeric forms of the T3SS inner rod proteins are partially folded.
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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.