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Interaction of the Yersinia pestis type III regulatory proteins LcrG and LcrV occurs at a hydrophobic interface.
Interaction of the Yersinia pestis type III regulatory proteins LcrG and LcrV occurs at a hydrophobic interface.
- Source :
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BMC microbiology [BMC Microbiol] 2002 Jun 28; Vol. 2, pp. 16. Date of Electronic Publication: 2002 Jun 28. - Publication Year :
- 2002
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Abstract
- Background: Secretion of anti-host proteins by Yersinia pestis via a type III mechanism is not constitutive. The process is tightly regulated and secretion occurs only after an appropriate signal is received. The interaction of LcrG and LcrV has been demonstrated to play a pivotal role in secretion control. Previous work has shown that when LcrG is incapable of interacting with LcrV, secretion of anti-host proteins is prevented. Therefore, an understanding of how LcrG interacts with LcrV is required to evaluate how this interaction regulates the type III secretion system of Y. pestis. Additionally, information about structure-function relationships within LcrG is necessary to fully understand the role of this key regulatory protein.<br />Results: In this study we demonstrate that the N-terminus of LcrG is required for interaction with LcrV. The interaction likely occurs within a predicted amphipathic coiled-coil domain within LcrG. Our results demonstrate that the hydrophobic face of the putative helix is required for LcrV interaction. Additionally, we demonstrate that the LcrG homolog, PcrG, is incapable of blocking type III secretion in Y. pestis. A genetic selection was utilized to obtain a PcrG variant capable of blocking secretion. This PcrG variant allowed us to locate a region of LcrG involved in secretion blocking.<br />Conclusion: Our results demonstrate that LcrG interacts with LcrV via hydrophobic interactions located in the N-terminus of LcrG within a predicted coiled-coil motif. We also obtained preliminary evidence that the secretion blocking activity of LcrG is located between amino acids 39 and 53.
- Subjects :
- Alanine genetics
Alanine physiology
Amino Acid Substitution genetics
Amino Acid Substitution physiology
Antigens, Bacterial physiology
Bacterial Proteins genetics
Bacterial Proteins physiology
Bacterial Typing Techniques
Genetic Variation
Hydrophobic and Hydrophilic Interactions
Leucine genetics
Leucine physiology
Mutagenesis, Site-Directed
Phenylalanine genetics
Phenylalanine physiology
Plague metabolism
Plague pathology
Pore Forming Cytotoxic Proteins
Protein Interaction Mapping methods
Protein Structure, Secondary
Sequence Homology, Amino Acid
Yersinia pestis chemistry
Yersinia pestis pathogenicity
Antigens, Bacterial metabolism
Bacterial Proteins metabolism
Yersinia pestis metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1471-2180
- Volume :
- 2
- Database :
- MEDLINE
- Journal :
- BMC microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 12102728
- Full Text :
- https://doi.org/10.1186/1471-2180-2-16