| Purification and Characterization of Legionella U-Box-Type E3 Ubiquitin Ligase. | |
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MedLine Citation:
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PMID: 23150407 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Bacterial virulence proteins often mimic host eukaryotic proteins to modify or disturb host cellular -pathways. Increasing lines of evidence show that many bacterial effector proteins have E3 ubiquitin ligase activity. The effector protein LubX is one such bacterial E3 ubiquitin ligase. We describe here the method to purify soluble LubX protein using GST-tag and Escherichia coli overexpression systems. Using the purified protein together with recombinant ubiquitin, E1, and E2 enzymes, ubiquitin ligase activity is analyzed by the in vitro ubiquitination assay. |
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Authors:
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Hiroki Nagai; Tomoko Kubori |
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Publication Detail:
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Type: JOURNAL ARTICLE |
Journal Detail:
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Title: Methods in molecular biology (Clifton, N.J.) Volume: 954 ISSN: 1940-6029 ISO Abbreviation: Methods Mol. Biol. Publication Date: 2013 |
Date Detail:
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Created Date: 2012-11-14 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9214969 Medline TA: Methods Mol Biol Country: - |
Other Details:
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Languages: ENG Pagination: 347-354 Citation Subset: - |
Affiliation:
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Research Institute for Microbial Diseases, Osaka University, Osaka, Japan, hnagai@biken.osaka-u.ac.jp. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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