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TitleA polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion.
Journal, issue, pagesPLoS Biol., Vol. 17, Issue 7, Page e3000351, Year 2019
Publish dateJul 1, 2019
AuthorsEmily Z Guo / Daniel C Desrosiers / Jan Zalesak / James Tolchard / Mélanie Berbon / Birgit Habenstein / Thomas Marlovits / Antoine Loquet / Jorge E Galán /
PubMed AbstractType III protein-secretion machines are essential for the interactions of many pathogenic or symbiotic bacterial species with their respective eukaryotic hosts. The core component of these machines ...Type III protein-secretion machines are essential for the interactions of many pathogenic or symbiotic bacterial species with their respective eukaryotic hosts. The core component of these machines is the injectisome, a multiprotein complex that mediates the selection of substrates, their passage through the bacterial envelope, and ultimately their delivery into eukaryotic target cells. The injectisome is composed of a large cytoplasmic complex or sorting platform, a multiring base embedded in the bacterial envelope, and a needle-like filament that protrudes several nanometers from the bacterial surface and is capped at its distal end by the tip complex. A characteristic feature of these machines is that their activity is stimulated by contact with target host cells. The sensing of target cells, thought to be mediated by the distal tip of the needle filament, generates an activating signal that must be transduced to the secretion machine by the needle filament. Here, through a multidisciplinary approach, including solid-state NMR (SSNMR) and cryo electron microscopy (cryo-EM) analyses, we have identified critical residues of the needle filament protein of a Salmonella Typhimurium type III secretion system that are involved in the regulation of the activity of the secretion machine. We found that mutations in the needle filament protein result in various specific phenotypes associated with different steps in the type III secretion process. More specifically, these studies reveal an important role for a polymorphic helix of the needle filament protein and the residues that line the lumen of its central channel in the control of type III secretion.
External linksPubMed:31260457 / Publisher's page
KeywordsBacterial Proteins / Bacterial Secretion Systems / Cryoelectron Microscopy / Models, Molecular / Multiprotein Complexes / Mutation / Protein Conformation / Protein Transport / Salmonella typhimurium / Type III Secretion Systems / Type III secretion / helical reconstruction / PrgI filament / salmonella / Type III secretion system
MethodsEM (helical sym.)
Resolution2.9 - 3.7 A
Structure data

EMDB-20043:
Helical reconstruction of Type III Secretion System Needle filament mutant-PrgI S49A

EMDB-20044:
High-resolution filamentous structures of in vitro polymerized PrgI needle

EMDB-20045:
In vitro polymerized PrgI V67A filaments

EMDB-20046:
Structure of Salmonella type III secretion system needle filament

PDB-6ofe:
Helical reconstruction of Type III Secretion System Needle filament mutant-PrgI S49A

PDB-6off:
High-resolution filamentous structures of in vitro polymerized PrgI needle

PDB-6ofg:
In vitro polymerized PrgI V67A filaments

PDB-6ofh:
Structure of Salmonella type III secretion system needle filament

Source
  • salmonella typhimurium (strain sl1344) (bacteria)
  • Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)

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