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Reciprocal secretion of proteins by the bacterial type III machines of plant and animal pathogens suggests universal recognition of mRNA targeting signals.
- Source :
-
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 1999 Oct 26; Vol. 96 (22), pp. 12839-43. - Publication Year :
- 1999
-
Abstract
- Bacterial pathogens of both animals and plants use type III secretion machines to inject virulence proteins into host cells. Although many components of the secretion machinery are conserved among different bacterial species, the substrates for their type III pathways are not. The Yersinia type III machinery recognizes some secretion substrates via a signal that is encoded within the first 15 codons of yop mRNA. These signals can be altered by frameshift mutations without affecting secretion of the encoded polypeptides, suggesting a mechanism whereby translation of yop mRNA is coupled to the translocation of newly synthesized polypeptide. We report that the type III machinery of Erwinia chrysanthemi cloned in Escherichia coli recognizes the secretion signals of yopE and yopQ. Pseudomonas syringae AvrB and AvrPto, two proteins exported by the recombinant Erwinia machine, can also be secreted by the Yersinia type III pathway. Mapping AvrPto sequences sufficient for the secretion of reporter fusions in Yersinia revealed the presence of an mRNA secretion signal. We propose that 11 conserved components of type III secretion machines may recognize signals that couple mRNA translation to polypeptide secretion.
- Subjects :
- Bacterial Proteins genetics
Bacterial Proteins metabolism
Base Sequence
DNA Primers
Dickeya chrysanthemi pathogenicity
Nucleic Acid Conformation
Pseudomonas pathogenicity
RNA, Messenger chemistry
RNA, Messenger genetics
Substrate Specificity
Yersinia pathogenicity
Dickeya chrysanthemi metabolism
Pseudomonas metabolism
RNA, Messenger metabolism
Signal Transduction
Yersinia metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0027-8424
- Volume :
- 96
- Issue :
- 22
- Database :
- MEDLINE
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Academic Journal
- Accession number :
- 10536009
- Full Text :
- https://doi.org/10.1073/pnas.96.22.12839