DOI: 10.1073/pnas.200209497. Contribution of <i>Salmonella typhimurium</i> type III secretion components to needle complex formation

Contribution of Salmonella typhimurium type III secretion components to needle complex formation

10.1073/pnas.200209497

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

The prgHIJK operon encodes components of the Salmonella typhimurium pathogenicity island 1 type III secretion system (TTSS). Previously, prgH and prgK were shown to be required for formation of the supramolecular type III secretion needle complex (NC) [Kubori, T., et al. (1998) Science 280, 602–605]. This work indicates that all prg operon genes are required for NC formation. PrgH multimerizes into a distinct tetrameric-shaped structure that may be an early intermediate of NC assembly and may provide the structural foundation required for PrgK oligomerization. PrgH and PrgK, in the absence of other TTSS components, oligomerize into ring-shaped structures identical in appearance and size to the base of the NC, indicating that they are likely the major inner membrane structural components required for secretion. PrgI and PrgJ cofractionate with the NC and are secreted into the culture supernatant. NC from prgI and prgJ mutants have an identical morphology to the envelope-spanning (basal body) NC components, but are missing the external needle, indicating that PrgI and PrgJ are required for full NC assembly and are likely components of the external needle. Therefore, PrgI and PrgJ are secreted through the NC basal body, composed in part of PrgH/K and InvG/H rings, to participate in assembly of the more distal components of the NC.

Bibliography

Kimbrough, T. G., & Miller, S. I. (2000). Contribution of Salmonella typhimurium type III secretion components to needle complex formation. Proceedings of the National Academy of Sciences, 97(20), 11008â11013.

Authors 2

Tyler G. Kimbrough (first)
Samuel I. Miller (additional)

References 22 Referenced 200

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Dates

Type	When
Created	23 years ago (July 26, 2002, 10:40 a.m.)
Deposited	3 years, 4 months ago (April 13, 2022, 6:45 a.m.)
Indexed	11 months, 3 weeks ago (Aug. 28, 2024, 9:48 a.m.)
Issued	24 years, 11 months ago (Sept. 12, 2000)
Published	24 years, 11 months ago (Sept. 12, 2000)
Published Online	24 years, 11 months ago (Sept. 12, 2000)
Published Print	24 years, 10 months ago (Sept. 26, 2000)

Funders 0

None

BibTeX

@article{Kimbrough_2000, title={Contribution of Salmonella typhimurium type III secretion components to needle complex formation}, volume={97}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.200209497}, DOI={10.1073/pnas.200209497}, number={20}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Kimbrough, Tyler G. and Miller, Samuel I.}, year={2000}, month=sep, pages={11008–11013} }

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  "abstract": "<jats:p>\n            The\n            <jats:italic>prgHIJK</jats:italic>\n            operon encodes components of the\n            <jats:italic>Salmonella typhimurium</jats:italic>\n            pathogenicity island 1 type III\n secretion system (TTSS). Previously,\n            <jats:italic>prgH</jats:italic>\n            and\n            <jats:italic>prgK</jats:italic>\n            were shown to be required for formation of the\n supramolecular type III secretion needle complex (NC) [Kubori, T.,\n            <jats:italic>et al.</jats:italic>\n            (1998)\n            <jats:italic>Science</jats:italic>\n            280, 602\u2013605].\n This work indicates that all\n            <jats:italic>prg</jats:italic>\n            operon genes are\n required for NC formation. PrgH multimerizes into a distinct\n tetrameric-shaped structure that may be an early intermediate of NC\n assembly and may provide the structural foundation required for PrgK\n oligomerization. PrgH and PrgK, in the absence of other TTSS\n components, oligomerize into ring-shaped structures identical in\n appearance and size to the base of the NC, indicating that they are\n likely the major inner membrane structural components required for\n secretion. PrgI and PrgJ cofractionate with the NC and are secreted\n into the culture supernatant. NC from\n            <jats:italic>prgI</jats:italic>\n            and\n            <jats:italic>prgJ</jats:italic>\n            mutants have an identical morphology to the\n envelope-spanning (basal body) NC components, but are missing the\n external needle, indicating that PrgI and PrgJ are required for full NC\n assembly and are likely components of the external needle. Therefore,\n PrgI and PrgJ are secreted through the NC basal body, composed in part\n of PrgH/K and InvG/H rings, to participate in assembly of the more\n distal components of the NC.\n          </jats:p>",
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