title: Synthesis and localization of the Salmonella SPI-1 type III secretion needle complex proteins PrgI and PrgJ.
abstract: An essential component of type III secretion systems (TTSS) is a supramolecular structure termed the needle complex. In Salmonella enterica, at least four proteins make up this structure: InvG, PrgH, PrgK, and PrgI. Another protein, PrgJ, is thought to play a role in the assembly of this structure, but its function is poorly understood. We have analyzed the expression and localization of PrgJ and the needle protein PrgI in different S. enterica serovar Typhimurium mutant strains. We found that the levels of PrgI and PrgJ were significantly reduced in a TTSS-deficient invA mutant strain and that the decreased levels were due to protein instability. In addition, we found that PrgJ, although associated with the needle complex in wild-type S. enterica serovar Typhimurium, was absent from needle complexes obtained from an invJ mutant strain, which exhibits very long needle substructures. We suggest that PrgJ is involved in capping the needle substructure of the needle complex.
authors.affiliation: Section of Microbial Pathogenesis, Yale School of Medicine, New Haven, Connecticut 06536-1418, USA.
authors.forename: Anand
authors.initials: A
authors.lastname: Sukhan
authors.forename: Tomoko
authors.initials: T
authors.lastname: Kubori
authors.forename: Jorge E
authors.initials: JE
authors.lastname: Galán
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003470:Culture Media; D009154:Mutation; D012486:Salmonella typhimurium / Q000235:genetics / Q000254:growth & development / Q000378:metabolism* / Q000472:pathogenicity*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014158:Transcription, Genetic; D014774:Virulence
chemical_list: D001426:Bacterial Proteins; D003470:Culture Media