| YopK controls both rate and fidelity of Yop translocation. | |
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MedLine Citation:
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PMID: 23205707 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Yersinia pestis, the causative agent of plague, utilizes a type III secretion system (T3SS) to intoxicate host cells. The injection of T3SS substrates must be carefully controlled, and dysregulation leads to altered infection kinetics and early clearance of Y. pestis. While the sequence of events leading up to cell contact and initiation of translocation has received much attention, the regulatory events that take place after effector translocation is less understood. Here we show that the regulator YopK is required to maintain fidelity of substrate specificity, in addition to controlling translocation rate. YopK was found to interact with YopD within targeted cells during Y. pestis infection, suggesting that YopK's regulatory mechanism involves a direct interaction with the translocation pore. In addition, we identified a single amino acid in YopK that is essential for translocation rate regulation but is dispensable for maintaining fidelity of translocation. Furthermore, we found that expression of YopK within host cells was sufficient to downregulate translocation rate, but it did not affect translocation fidelity. Together, our data support a model in which YopK is a bifunctional protein whose activities are genetically and spatially distinct such that fidelity control occurs within bacteria and rate control occurs within host cells. |
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Authors:
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Rebecca Dewoody; Peter M Merritt; Melanie M Marketon |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-12-4 |
Journal Detail:
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Title: Molecular microbiology Volume: - ISSN: 1365-2958 ISO Abbreviation: Mol. Microbiol. Publication Date: 2012 Dec |
Date Detail:
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Created Date: 2012-12-4 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8712028 Medline TA: Mol Microbiol Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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© 2012 Blackwell Publishing Ltd. |
Affiliation:
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Department of Biology, Indiana University, Bloomington, IN, 47405, USA. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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