Reversible Unfolding of the Severe Acute Respiratory Syndrome Coronavirus Main Protease in Guanidinium Chloride
Identifieur interne : 003613 ( Main/Exploration ); précédent : 003612; suivant : 003614Reversible Unfolding of the Severe Acute Respiratory Syndrome Coronavirus Main Protease in Guanidinium Chloride
Auteurs : Hui-Ping Chang ; Chi-Yuan Chou ; Gu-Gang ChangSource :
- Biophysical Journal [ 0006-3495 ] ; 2007.
Descripteurs français
- KwdFr :
- Cysteine endopeptidases (), Dichroïsme circulaire, Domaine catalytique, Dénaturation des protéines, Guanidine (), Indicateurs et réactifs, Modèles moléculaires, Pliage des protéines, Protéines virales (), Sites de fixation, Structure quaternaire des protéines, Structure tertiaire des protéines, Virus du SRAS (enzymologie).
- MESH :
- enzymologie : Virus du SRAS.
- Cysteine endopeptidases, Dichroïsme circulaire, Domaine catalytique, Dénaturation des protéines, Guanidine, Indicateurs et réactifs, Modèles moléculaires, Pliage des protéines, Protéines virales, Sites de fixation, Structure quaternaire des protéines, Structure tertiaire des protéines.
English descriptors
- KwdEn :
- Binding Sites, Catalytic Domain, Circular Dichroism, Cysteine Endopeptidases (chemistry), Guanidine (chemistry), Indicators and Reagents, Models, Molecular, Protein Denaturation, Protein Folding, Protein Structure, Quaternary, Protein Structure, Tertiary, SARS Virus (enzymology), Viral Proteins (chemistry).
- MESH :
- chemical , chemistry : Cysteine Endopeptidases, Guanidine, Viral Proteins.
- enzymology : SARS Virus.
- Binding Sites, Catalytic Domain, Circular Dichroism, Indicators and Reagents, Models, Molecular, Protein Denaturation, Protein Folding, Protein Structure, Quaternary, Protein Structure, Tertiary.
Abstract
Chemical denaturant sensitivity of the dimeric main protease from severe acute respiratory syndrome (SARS) coronavirus to guanidinium chloride was examined in terms of fluorescence spectroscopy, circular dichroism, analytical ultracentrifuge, and enzyme activity change. The dimeric enzyme dissociated at guanidinium chloride concentration of <0.4 M, at which the enzymatic activity loss showed close correlation with the subunit dissociation. Further increase in guanidinium chloride induced a reversible biphasic unfolding of the enzyme. The unfolding of the C-terminal domain-truncated enzyme, on the other hand, followed a monophasic unfolding curve. Different mutants of the full-length protease (W31 and W207/W218), with tryptophanyl residue(s) mutated to phenylalanine at the C-terminal or N-terminal domain, respectively, were constructed. Unfolding curves of these mutants were monophasic but corresponded to the first and second phases of the protease, respectively. The unfolding intermediate of the protease thus represented a folded C-terminal domain but an unfolded N-terminal domain, which is enzymatically inactive due to loss of regulatory properties. The various enzyme forms were characterized in terms of hydrophobicity and size-and-shape distributions. We provide direct evidence for the functional role of C-terminal domain in stabilization of the catalytic N-terminal domain of SARS coronavirus main protease.
Url:
DOI: 10.1529/biophysj.106.091736
PubMed: 17142288
PubMed Central: 1783898
Affiliations:
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Le document en format XML
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type="wicri:Area/Ncbi/Checkpoint">001788</idno><idno type="wicri:doubleKey">0006-3495:2007:Chang H:reversible:unfolding:of</idno><idno type="wicri:Area/Main/Merge">003740</idno><idno type="wicri:Area/Main/Curation">003613</idno><idno type="wicri:Area/Main/Exploration">003613</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Reversible Unfolding of the Severe Acute Respiratory Syndrome Coronavirus Main Protease in Guanidinium Chloride</title><author><name sortKey="Chang, Hui Ping" sort="Chang, Hui Ping" uniqKey="Chang H" first="Hui-Ping" last="Chang">Hui-Ping Chang</name></author><author><name sortKey="Chou, Chi Yuan" sort="Chou, Chi Yuan" uniqKey="Chou C" first="Chi-Yuan" last="Chou">Chi-Yuan Chou</name></author><author><name sortKey="Chang, Gu Gang" sort="Chang, Gu Gang" uniqKey="Chang G" first="Gu-Gang" last="Chang">Gu-Gang Chang</name></author></analytic><series><title level="j">Biophysical Journal</title><idno type="ISSN">0006-3495</idno><idno type="eISSN">1542-0086</idno><imprint><date when="2007">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites</term><term>Catalytic Domain</term><term>Circular Dichroism</term><term>Cysteine Endopeptidases (chemistry)</term><term>Guanidine (chemistry)</term><term>Indicators and Reagents</term><term>Models, Molecular</term><term>Protein Denaturation</term><term>Protein Folding</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Tertiary</term><term>SARS Virus (enzymology)</term><term>Viral Proteins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cysteine endopeptidases ()</term><term>Dichroïsme circulaire</term><term>Domaine catalytique</term><term>Dénaturation des protéines</term><term>Guanidine ()</term><term>Indicateurs et réactifs</term><term>Modèles moléculaires</term><term>Pliage des protéines</term><term>Protéines virales ()</term><term>Sites de fixation</term><term>Structure quaternaire des protéines</term><term>Structure tertiaire des protéines</term><term>Virus du SRAS (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Guanidine</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Catalytic Domain</term><term>Circular Dichroism</term><term>Indicators and Reagents</term><term>Models, Molecular</term><term>Protein Denaturation</term><term>Protein Folding</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cysteine endopeptidases</term><term>Dichroïsme circulaire</term><term>Domaine catalytique</term><term>Dénaturation des protéines</term><term>Guanidine</term><term>Indicateurs et réactifs</term><term>Modèles moléculaires</term><term>Pliage des protéines</term><term>Protéines virales</term><term>Sites de fixation</term><term>Structure quaternaire des protéines</term><term>Structure tertiaire des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Chemical denaturant sensitivity of the dimeric main protease from severe acute respiratory syndrome (SARS) coronavirus to guanidinium chloride was examined in terms of fluorescence spectroscopy, circular dichroism, analytical ultracentrifuge, and enzyme activity change. The dimeric enzyme dissociated at guanidinium chloride concentration of <0.4 M, at which the enzymatic activity loss showed close correlation with the subunit dissociation. Further increase in guanidinium chloride induced a reversible biphasic unfolding of the enzyme. The unfolding of the C-terminal domain-truncated enzyme, on the other hand, followed a monophasic unfolding curve. Different mutants of the full-length protease (W31 and W207/W218), with tryptophanyl residue(s) mutated to phenylalanine at the C-terminal or N-terminal domain, respectively, were constructed. Unfolding curves of these mutants were monophasic but corresponded to the first and second phases of the protease, respectively. The unfolding intermediate of the protease thus represented a folded C-terminal domain but an unfolded N-terminal domain, which is enzymatically inactive due to loss of regulatory properties. The various enzyme forms were characterized in terms of hydrophobicity and size-and-shape distributions. We provide direct evidence for the functional role of C-terminal domain in stabilization of the catalytic N-terminal domain of SARS coronavirus main protease.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Chan, H L" uniqKey="Chan H">H.L. Chan</name></author><author><name sortKey="Tsui, S K" uniqKey="Tsui S">S.K. Tsui</name></author><author><name sortKey="Sung, J J" uniqKey="Sung J">J.J. Sung</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Matsuyama, S" uniqKey="Matsuyama S">S. Matsuyama</name></author><author><name sortKey="Ujike, M" uniqKey="Ujike M">M. Ujike</name></author><author><name sortKey="Morikawa, S" uniqKey="Morikawa S">S. Morikawa</name></author><author><name sortKey="Tashiro, M" uniqKey="Tashiro M">M. 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Gruebele</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Lindorff Larsen, K" uniqKey="Lindorff Larsen K">K. Lindorff-Larsen</name></author><author><name sortKey="Rogen, P" uniqKey="Rogen P">P. Rogen</name></author><author><name sortKey="Paci, E" uniqKey="Paci E">E. Paci</name></author><author><name sortKey="Vendruscolo, M" uniqKey="Vendruscolo M">M. Vendruscolo</name></author><author><name sortKey="Dobson, C M" uniqKey="Dobson C">C.M. Dobson</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Oliveberg, M" uniqKey="Oliveberg M">M. Oliveberg</name></author><author><name sortKey="Shakhnovich, E I" uniqKey="Shakhnovich E">E.I. Shakhnovich</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Shi, J" uniqKey="Shi J">J. Shi</name></author><author><name sortKey="Song, J" uniqKey="Song J">J. Song</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Delano, W L" uniqKey="Delano W">W.L. DeLano</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list></list><tree><noCountry><name sortKey="Chang, Gu Gang" sort="Chang, Gu Gang" uniqKey="Chang G" first="Gu-Gang" last="Chang">Gu-Gang Chang</name><name sortKey="Chang, Hui Ping" sort="Chang, Hui Ping" uniqKey="Chang H" first="Hui-Ping" last="Chang">Hui-Ping Chang</name><name sortKey="Chou, Chi Yuan" sort="Chou, Chi Yuan" uniqKey="Chou C" first="Chi-Yuan" last="Chou">Chi-Yuan Chou</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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