
Role of the Hrp pilus in type III protein secretion in Pseudomonas syringae.
Publication
, Journal Article
Jin, Q; He, SY
Published in: Science (New York, N.Y.)
December 2001
Bacterial surface appendages called pili and needle-like filaments are associated with protein and/or DNA transfer to recipient plant, human, or bacterial cells during pathogenesis or conjugation. Although it has long been suspected that pili function as a conduit for protein or DNA transfer, direct evidence has been lacking. The Hrp pilus of Pseudomonas syringae is assembled by the type III secretion system. We used an in situ immunogold labeling procedure to visualize the extrusion of an effector protein, AvrPto, from the tip of the Hrp pilus, providing direct evidence that a bacterial pilus can function as a conduit for protein delivery.
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Published In
Science (New York, N.Y.)
DOI
EISSN
1095-9203
ISSN
0036-8075
Publication Date
December 2001
Volume
294
Issue
5551
Start / End Page
2556 / 2558
Related Subject Headings
- RNA Helicases
- Pseudomonas
- Polysaccharide-Lyases
- Microscopy, Immunoelectron
- Immunohistochemistry
- General Science & Technology
- Fimbriae, Bacterial
- Escherichia coli Proteins
- DEAD-box RNA Helicases
- Bacterial Proteins
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Jin, Q., & He, S. Y. (2001). Role of the Hrp pilus in type III protein secretion in Pseudomonas syringae. Science (New York, N.Y.), 294(5551), 2556–2558. https://doi.org/10.1126/science.1066397
Jin, Q., and S. Y. He. “Role of the Hrp pilus in type III protein secretion in Pseudomonas syringae.” Science (New York, N.Y.) 294, no. 5551 (December 2001): 2556–58. https://doi.org/10.1126/science.1066397.
Jin Q, He SY. Role of the Hrp pilus in type III protein secretion in Pseudomonas syringae. Science (New York, NY). 2001 Dec;294(5551):2556–8.
Jin, Q., and S. Y. He. “Role of the Hrp pilus in type III protein secretion in Pseudomonas syringae.” Science (New York, N.Y.), vol. 294, no. 5551, Dec. 2001, pp. 2556–58. Epmc, doi:10.1126/science.1066397.
Jin Q, He SY. Role of the Hrp pilus in type III protein secretion in Pseudomonas syringae. Science (New York, NY). 2001 Dec;294(5551):2556–2558.

Published In
Science (New York, N.Y.)
DOI
EISSN
1095-9203
ISSN
0036-8075
Publication Date
December 2001
Volume
294
Issue
5551
Start / End Page
2556 / 2558
Related Subject Headings
- RNA Helicases
- Pseudomonas
- Polysaccharide-Lyases
- Microscopy, Immunoelectron
- Immunohistochemistry
- General Science & Technology
- Fimbriae, Bacterial
- Escherichia coli Proteins
- DEAD-box RNA Helicases
- Bacterial Proteins