| The prodomain of the Bordetella two-partner secretion pathway protein FhaB remains intracellular yet affects the conformation of the mature C-terminal domain. | |
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MedLine Citation:
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PMID: 23035892 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Two-partner secretion (TPS) systems use β-barrel proteins of the Omp85-TpsB superfamily to transport large exoproteins across the outer membranes of Gram-negative bacteria. The Bordetella FHA/FhaC proteins are prototypical of TPS systems in which the exoprotein contains a large C-terminal prodomain that is removed during translocation. Although it is known that the FhaB prodomain is required for FHA function in vivo, its role in FHA maturation has remained mysterious. We show here that the FhaB prodomain is required for the extracellularly located mature C-terminal domain (MCD) of FHA to achieve its proper conformation. We show that the C-terminus of the prodomain is retained intracellularly and that sequences within the N-terminus of the prodomain are required for this intracellular localization. We also identify sequences at the C-terminus of the MCD that are required for release of mature FHA from the cell surface. Our data support a model in which the intracellularly located prodomain affects the final conformation of the extracellularly located MCD. We hypothesize that maturation triggers cleavage and degradation of the prodomain. |
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Authors:
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Christopher R Noël; Joseph Mazar; Jeffrey A Melvin; Jessica A Sexton; Peggy A Cotter |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-10-5 |
Journal Detail:
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Title: Molecular microbiology Volume: - ISSN: 1365-2958 ISO Abbreviation: Mol. Microbiol. Publication Date: 2012 Oct |
Date Detail:
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Created Date: 2012-10-5 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 Microbiology and Immunology, School of Medicine, University of North Carolina, Chapel Hill, NC, 27599-7290, USA; Biomolecular Sciences and Engineering Program, University of California, Santa Barbara, CA, 93106-9610, USA. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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