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Reversible Unfolding of the Severe Acute Respiratory Syndrome Coronavirus Main Protease in Guanidinium Chloride

Identifieur interne : 000199 ( Pmc/Curation ); précédent : 000198; suivant : 000200

Reversible Unfolding of the Severe Acute Respiratory Syndrome Coronavirus Main Protease in Guanidinium Chloride

Auteurs : Hui-Ping Chang ; Chi-Yuan Chou ; Gu-Gang Chang

Source :

RBID : PMC:1783898

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

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PMC:1783898

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<title xml:lang="en">Reversible Unfolding of the Severe Acute Respiratory Syndrome Coronavirus Main Protease in Guanidinium Chloride</title>
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<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>
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<author>
<name sortKey="Chang, Gu Gang" sort="Chang, Gu Gang" uniqKey="Chang G" first="Gu-Gang" last="Chang">Gu-Gang Chang</name>
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<title xml:lang="en" level="a" type="main">Reversible Unfolding of the Severe Acute Respiratory Syndrome Coronavirus Main Protease in Guanidinium Chloride</title>
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<name sortKey="Chang, Hui Ping" sort="Chang, Hui Ping" uniqKey="Chang H" first="Hui-Ping" last="Chang">Hui-Ping Chang</name>
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<name sortKey="Chou, Chi Yuan" sort="Chou, Chi Yuan" uniqKey="Chou C" first="Chi-Yuan" last="Chou">Chi-Yuan Chou</name>
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<name sortKey="Chang, Gu Gang" sort="Chang, Gu Gang" uniqKey="Chang G" first="Gu-Gang" last="Chang">Gu-Gang Chang</name>
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<title level="j">Biophysical Journal</title>
<idno type="ISSN">0006-3495</idno>
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<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>
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<pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front>
<journal-meta>
<journal-id journal-id-type="nlm-ta">Biophys J</journal-id>
<journal-id journal-id-type="publisher-id">biophysj</journal-id>
<journal-title>Biophysical Journal</journal-title>
<issn pub-type="ppub">0006-3495</issn>
<issn pub-type="epub">1542-0086</issn>
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<article-id pub-id-type="doi">10.1529/biophysj.106.091736</article-id>
<article-categories>
<subj-group subj-group-type="heading">
<subject>Proteins</subject>
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<title-group>
<article-title>Reversible Unfolding of the Severe Acute Respiratory Syndrome Coronavirus Main Protease in Guanidinium Chloride</article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname>Chang</surname>
<given-names>Hui-Ping</given-names>
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<contrib contrib-type="author">
<name>
<surname>Chou</surname>
<given-names>Chi-Yuan</given-names>
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<contrib contrib-type="author">
<name>
<surname>Chang</surname>
<given-names>Gu-Gang</given-names>
</name>
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<aff id="N0xa393b08N0xa3a43e0">Department of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, Taipei, Taiwan</aff>
<author-notes>
<fn>
<p>Address reprint requests to Hui-Ping Chang, Dept. of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, 155 Li-Nong St., Section 2, Taipei 112, Taiwan. E-mail:
<email>huiping_chp@hotmail.com</email>
.</p>
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<pub-date pub-type="ppub">
<day>15</day>
<month>2</month>
<year>2007</year>
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<pub-date pub-type="epub">
<day>1</day>
<month>12</month>
<year>2006</year>
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<volume>92</volume>
<issue>4</issue>
<fpage>1374</fpage>
<lpage>1383</lpage>
<history>
<date date-type="received">
<day>19</day>
<month>6</month>
<year>2006</year>
</date>
<date date-type="accepted">
<day>2</day>
<month>11</month>
<year>2006</year>
</date>
</history>
<copyright-statement>Copyright © 2007, Biophysical Society</copyright-statement>
<copyright-year>2007</copyright-year>
<abstract>
<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>
</abstract>
</article-meta>
<notes>
<fn-group>
<fn>
<p>
<italic>Abbreviations used</italic>
: SARS, severe acute respiratory syndrome; CoV, coronavirus; 3CLpro, 3-chymotrypsin-like SARS-CoV main protease; 3CL
<sub>I+II</sub>
, C-terminal domain-truncated SARS-CoV main protease; W31 (or more precisely W207F/W218F), double mutant of SARS-CoV 3CLpro with tryptophanyl residues at 207 and 218 mutated to phenylalanine; W207/W218 (or more precisely W31F), point mutant of SARS-CoV 3CLpro with tryptophanyl residue at position 31 mutated to phenylalanine; AEW, average emission wavelength; CD, circular dichroism; AUC, analytical ultracentrifugation; GdnCl, guanidinium chloride;
<italic>f/f</italic>
<sub>o</sub>
, frictional ratio; ANS, 1-anilino-8-naphthalene sulfonic acid.</p>
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