Abstract
In this study, we report the simultaneous refolding and reconstitution of the recombinant Bax inhibitor-1 (BI-1) from inclusion bodies expressed in Escherichia coli. A functional assay showed that the resulting proteoliposomes responded to acidic conditions and triggered the release of entrapped Ca(2+) from liposomes. The secondary structure of the reconstituted BI-1 was also determined using circular dichroism, which revealed an increase of alpha-helix content and a decrease of random structure when exposed to acidic solutions. These conformational changes may be responsible for the proton ion-induced Ca(2+) release of BI-1.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Apoptosis Regulatory Proteins / chemistry
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Apoptosis Regulatory Proteins / genetics
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Apoptosis Regulatory Proteins / metabolism*
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Calcium / metabolism
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Escherichia coli / cytology
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Humans
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Hydrogen-Ion Concentration
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Inclusion Bodies / chemistry*
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Membrane Proteins / chemistry
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Membrane Proteins / genetics
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Membrane Proteins / metabolism*
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Protein Engineering
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Protein Folding
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Protein Structure, Secondary
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Proteolipids / chemistry*
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism*
Substances
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Apoptosis Regulatory Proteins
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Membrane Proteins
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Proteolipids
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Recombinant Fusion Proteins
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TMBIM6 protein, human
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proteoliposomes
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Calcium