| pubmed-article:15548616 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:15548616 | lifeskim:mentions | umls-concept:C1522702 | lld:lifeskim |
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| pubmed-article:15548616 | lifeskim:mentions | umls-concept:C0599893 | lld:lifeskim |
| pubmed-article:15548616 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:15548616 | lifeskim:mentions | umls-concept:C1550548 | lld:lifeskim |
| pubmed-article:15548616 | lifeskim:mentions | umls-concept:C1555714 | lld:lifeskim |
| pubmed-article:15548616 | lifeskim:mentions | umls-concept:C1548602 | lld:lifeskim |
| pubmed-article:15548616 | lifeskim:mentions | umls-concept:C1705654 | lld:lifeskim |
| pubmed-article:15548616 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:15548616 | lifeskim:mentions | umls-concept:C0964849 | lld:lifeskim |
| pubmed-article:15548616 | pubmed:issue | 48 | lld:pubmed |
| pubmed-article:15548616 | pubmed:dateCreated | 2004-12-1 | lld:pubmed |
| pubmed-article:15548616 | pubmed:abstractText | Entry of the enzymatic components of anthrax toxin [lethal factor (LF) and edema factor] into the cytosol of mammalian cells depends on the ability of the activated protective antigen (PA63) component to form a channel (pore) in the membrane of an acidic intracellular compartment. To investigate the mechanism of translocation, we characterized N-terminally truncated forms of the PA63-binding domain of LF (LFN). Deleting 27 or 36 residues strongly inhibited acid-triggered translocation of LFN across the plasma membrane of CHO-K1 cells and ablated the protein's ability to block PA63 channels in planar lipid bilayers at a small positive voltage (+20 mV). Fusing a H6-tag to the N terminus of the truncated proteins restored both translocation and channel-blocking activities. At +20 mV, N-terminal H6 and biotin tags were accessible to Ni2+ and streptavidin, respectively, added to the trans compartment of a planar bilayer. On the basis of these findings, we propose that the N terminus of PA63-bound LF or edema factor enters the PA63-channel under the influence of acidic pH and a positive transmembrane potential and initiates translocation in an N- to C-terminal direction. | lld:pubmed |
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| pubmed-article:15548616 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15548616 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15548616 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15548616 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:15548616 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:15548616 | pubmed:author | pubmed-author:CollierR... | lld:pubmed |
| pubmed-article:15548616 | pubmed:author | pubmed-author:FinkelsteinAl... | lld:pubmed |
| pubmed-article:15548616 | pubmed:author | pubmed-author:ZhangSenS | lld:pubmed |
| pubmed-article:15548616 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15548616 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:15548616 | pubmed:volume | 101 | lld:pubmed |
| pubmed-article:15548616 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15548616 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15548616 | pubmed:pagination | 16756-61 | lld:pubmed |
| pubmed-article:15548616 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:15548616 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15548616 | pubmed:articleTitle | Evidence that translocation of anthrax toxin's lethal factor is initiated by entry of its N terminus into the protective antigen channel. | lld:pubmed |
| pubmed-article:15548616 | pubmed:affiliation | Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA. | lld:pubmed |
| pubmed-article:15548616 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15548616 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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