SrasV1, PubMed, Checkpoint, bibRecord, 002609

Mutational analysis of the SARS virus Nsp15 endoribonuclease: identification of residues affecting hexamer formation.

Identifieur interne : 002609 ( PubMed/Checkpoint ); précédent : 002608; suivant : 002610

Mutational analysis of the SARS virus Nsp15 endoribonuclease: identification of residues affecting hexamer formation.

Auteurs : Linda A. Guarino [États-Unis] ; Kanchan Bhardwaj ; Wen Dong ; Jingchuan Sun ; Andreas Holzenburg ; Cheng Kao

Source :

Journal of molecular biology [ 0022-2836 ] ; 2005.

RBID : pubmed:16216269

Descripteurs français

English descriptors

KwdEn :
- Amino Acids, Cloning, Molecular, DNA Mutational Analysis, Dimerization, Endoribonucleases (chemistry), Endoribonucleases (genetics), Endoribonucleases (metabolism), Kinetics, Microscopy, Electron, Transmission, Protein Structure, Secondary, SARS Virus (chemistry), Structure-Activity Relationship, Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism).
MESH :
- chemical , chemistry : Endoribonucleases, Viral Nonstructural Proteins.
- chemical , genetics : Endoribonucleases, Viral Nonstructural Proteins.
- chemical , metabolism : Endoribonucleases, Viral Nonstructural Proteins.
- chemical : Amino Acids.
- chemistry : SARS Virus.
- Cloning, Molecular, DNA Mutational Analysis, Dimerization, Kinetics, Microscopy, Electron, Transmission, Protein Structure, Secondary, Structure-Activity Relationship.

Abstract

The severe acute respiratory syndrome (SARS) coronavirus virus non-structural protein 15 is a Mn2+-dependent endoribonuclease with specificity for cleavage at uridylate residues. To better understand structural and functional characteristics of Nsp15, 22 mutant versions of Nsp15 were produced in Escherichia coli as His-tagged proteins and purified by metal-affinity and ion-exchange chromatography. Nineteen of the mutants were soluble and were analyzed for enzymatic activity. Six mutants, including four at the putative active site, were significantly reduced in endoribonuclease activity. Two of the inactive mutants had unusual secondary structures compared to the wild-type protein, as measured by circular dichroism spectroscopy. Gel-filtration analysis, velocity sedimentation ultracentrifugation, and native gradient pore electrophoresis all showed that the wild-type protein exists in an equilibrium between hexamers and monomers in solution, with hexamers dominating at micromolar protein concentration, while native gradient pore electrophoresis also revealed the presence of trimers. A mutant in the N terminus of Nsp15 was impaired in hexamer formation and had low endoribonuclease activity, suggesting that oligomerization is required for endoribonuclease activity. This idea was supported by titration experiments showing that enzyme activity was strongly concentration-dependent, indicating that oligomeric Nsp15 is the active form. Three-dimensional reconstruction of negatively stained single particles of Nsp15 viewed by transmission electron microscopic analysis suggested that the six subunits were arranged as a dimer of trimers with a number of cavities or channels that may constitute RNA binding sites.

DOI: 10.1016/j.jmb.2005.09.007
PubMed: 16216269

Affiliations:

États-Unis

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to stream PubMed, to step Corpus: 002508
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pubmed:16216269

Le document en format XML

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<term>Endoribonucleases ()</term>
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<term>Endoribonucleases (métabolisme)</term>
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<front><div type="abstract" xml:lang="en">The severe acute respiratory syndrome (SARS) coronavirus virus non-structural protein 15 is a Mn2+-dependent endoribonuclease with specificity for cleavage at uridylate residues. To better understand structural and functional characteristics of Nsp15, 22 mutant versions of Nsp15 were produced in Escherichia coli as His-tagged proteins and purified by metal-affinity and ion-exchange chromatography. Nineteen of the mutants were soluble and were analyzed for enzymatic activity. Six mutants, including four at the putative active site, were significantly reduced in endoribonuclease activity. Two of the inactive mutants had unusual secondary structures compared to the wild-type protein, as measured by circular dichroism spectroscopy. Gel-filtration analysis, velocity sedimentation ultracentrifugation, and native gradient pore electrophoresis all showed that the wild-type protein exists in an equilibrium between hexamers and monomers in solution, with hexamers dominating at micromolar protein concentration, while native gradient pore electrophoresis also revealed the presence of trimers. A mutant in the N terminus of Nsp15 was impaired in hexamer formation and had low endoribonuclease activity, suggesting that oligomerization is required for endoribonuclease activity. This idea was supported by titration experiments showing that enzyme activity was strongly concentration-dependent, indicating that oligomeric Nsp15 is the active form. Three-dimensional reconstruction of negatively stained single particles of Nsp15 viewed by transmission electron microscopic analysis suggested that the six subunits were arranged as a dimer of trimers with a number of cavities or channels that may constitute RNA binding sites.</div>
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<Abstract><AbstractText>The severe acute respiratory syndrome (SARS) coronavirus virus non-structural protein 15 is a Mn2+-dependent endoribonuclease with specificity for cleavage at uridylate residues. To better understand structural and functional characteristics of Nsp15, 22 mutant versions of Nsp15 were produced in Escherichia coli as His-tagged proteins and purified by metal-affinity and ion-exchange chromatography. Nineteen of the mutants were soluble and were analyzed for enzymatic activity. Six mutants, including four at the putative active site, were significantly reduced in endoribonuclease activity. Two of the inactive mutants had unusual secondary structures compared to the wild-type protein, as measured by circular dichroism spectroscopy. Gel-filtration analysis, velocity sedimentation ultracentrifugation, and native gradient pore electrophoresis all showed that the wild-type protein exists in an equilibrium between hexamers and monomers in solution, with hexamers dominating at micromolar protein concentration, while native gradient pore electrophoresis also revealed the presence of trimers. A mutant in the N terminus of Nsp15 was impaired in hexamer formation and had low endoribonuclease activity, suggesting that oligomerization is required for endoribonuclease activity. This idea was supported by titration experiments showing that enzyme activity was strongly concentration-dependent, indicating that oligomeric Nsp15 is the active form. Three-dimensional reconstruction of negatively stained single particles of Nsp15 viewed by transmission electron microscopic analysis suggested that the six subunits were arranged as a dimer of trimers with a number of cavities or channels that may constitute RNA binding sites.</AbstractText>
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<affiliations><list><country><li>États-Unis</li>
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<tree><noCountry><name sortKey="Bhardwaj, Kanchan" sort="Bhardwaj, Kanchan" uniqKey="Bhardwaj K" first="Kanchan" last="Bhardwaj">Kanchan Bhardwaj</name>
<name sortKey="Dong, Wen" sort="Dong, Wen" uniqKey="Dong W" first="Wen" last="Dong">Wen Dong</name>
<name sortKey="Holzenburg, Andreas" sort="Holzenburg, Andreas" uniqKey="Holzenburg A" first="Andreas" last="Holzenburg">Andreas Holzenburg</name>
<name sortKey="Kao, Cheng" sort="Kao, Cheng" uniqKey="Kao C" first="Cheng" last="Kao">Cheng Kao</name>
<name sortKey="Sun, Jingchuan" sort="Sun, Jingchuan" uniqKey="Sun J" first="Jingchuan" last="Sun">Jingchuan Sun</name>
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<country name="États-Unis"><noRegion><name sortKey="Guarino, Linda A" sort="Guarino, Linda A" uniqKey="Guarino L" first="Linda A" last="Guarino">Linda A. Guarino</name>
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   |texte=   Mutational analysis of the SARS virus Nsp15 endoribonuclease: identification of residues affecting hexamer formation.
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Mutational analysis of the SARS virus Nsp15 endoribonuclease: identification of residues affecting hexamer formation.

Mutational analysis of the SARS virus Nsp15 endoribonuclease: identification of residues affecting hexamer formation.

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