SrasV1, PubMed, Checkpoint, bibRecord, 001223

Autoprocessing mechanism of severe acute respiratory syndrome coronavirus 3C-like protease (SARS-CoV 3CLpro) from its polyproteins.

Identifieur interne : 001223 ( PubMed/Checkpoint ); précédent : 001222; suivant : 001224

Autoprocessing mechanism of severe acute respiratory syndrome coronavirus 3C-like protease (SARS-CoV 3CLpro) from its polyproteins.

Auteurs : Tomonari Muramatsu [Japon] ; Yong-Tae Kim ; Wataru Nishii ; Takaho Terada ; Mikako Shirouzu ; Shigeyuki Yokoyama

Source :

The FEBS journal [ 1742-4658 ] ; 2013.

RBID : pubmed:23452147

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Amino Acid Substitution, Cysteine Endopeptidases (biosynthesis), Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (genetics), Enzyme Assays, Escherichia coli, Green Fluorescent Proteins (biosynthesis), Green Fluorescent Proteins (chemistry), Kinetics, Mutagenesis, Site-Directed, Polyproteins (biosynthesis), Polyproteins (chemistry), Polyproteins (genetics), Protein Biosynthesis, Protein Precursors (biosynthesis), Protein Precursors (chemistry), Protein Precursors (genetics), Protein Processing, Post-Translational, Proteolysis, Recombinant Fusion Proteins (biosynthesis), Recombinant Fusion Proteins (chemistry), SARS Virus (enzymology), Viral Proteins (biosynthesis), Viral Proteins (chemistry), Viral Proteins (genetics).
MESH :
- chemical , biosynthesis : Cysteine Endopeptidases, Green Fluorescent Proteins, Polyproteins, Protein Precursors, Recombinant Fusion Proteins, Viral Proteins.
- chemical , chemistry : Cysteine Endopeptidases, Green Fluorescent Proteins, Polyproteins, Protein Precursors, Recombinant Fusion Proteins, Viral Proteins.
- chemical , genetics : Cysteine Endopeptidases, Polyproteins, Protein Precursors, Viral Proteins.
- enzymology : SARS Virus.
- Amino Acid Sequence, Amino Acid Substitution, Enzyme Assays, Escherichia coli, Kinetics, Mutagenesis, Site-Directed, Protein Biosynthesis, Protein Processing, Post-Translational, Proteolysis.

Abstract

Like many other RNA viruses, severe acute respiratory syndrome coronavirus (SARS-CoV) produces polyproteins containing several non-structural proteins, which are then processed by the viral proteases. These proteases often exist within the polyproteins, and are excised by their own proteolytic activity ('autoprocessing'). It is important to investigate the autoprocessing mechanism of these proteases from the point of view of anti-SARS-CoV drug design. In this paper, we describe a new method for investigating the autoprocessing mechanism of the main protease (M(pro)), which is also called the 3C-like protease (3CL(pro)). Using our method, we measured the activities, under the same conditions, of the mature form and pro-forms with the N-terminal pro-sequence, the C-terminal pro-sequence or both pro-sequences, toward the pro-form with both N- and C-terminal pro-sequences. The data indicate that the pro-forms of the enzyme have proteolytic activity, and are stimulated by the same proteolytic activity. The stimulation occurs in two steps, with approximately eightfold stimulation by N-terminal cleavage, approximately fourfold stimulation by C-terminal cleavage, and 23-fold stimulation by the cleavage of both termini, compared to the pro-form with both the N- and C-terminal pro-sequences. Such cleavage mainly occurs in a trans manner; i.e. the pro-form dimer cleaves the monomeric form. The stimulation by N-terminal pro-sequence removal is due to the cis (intra-dimer and inter-protomer) effect of formation of the new N-terminus, whereas that by C-terminal cleavage is due to removal of its trans (inter-dimer) inhibitory effect. A numerical simulation of the maturation pathway is presented.

DOI: 10.1111/febs.12222
PubMed: 23452147

Affiliations:

Japon

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 001245
to stream PubMed, to step Curation: 001245

Links to Exploration step

pubmed:23452147

Le document en format XML

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<front><div type="abstract" xml:lang="en">Like many other RNA viruses, severe acute respiratory syndrome coronavirus (SARS-CoV) produces polyproteins containing several non-structural proteins, which are then processed by the viral proteases. These proteases often exist within the polyproteins, and are excised by their own proteolytic activity ('autoprocessing'). It is important to investigate the autoprocessing mechanism of these proteases from the point of view of anti-SARS-CoV drug design. In this paper, we describe a new method for investigating the autoprocessing mechanism of the main protease (M(pro)), which is also called the 3C-like protease (3CL(pro)). Using our method, we measured the activities, under the same conditions, of the mature form and pro-forms with the N-terminal pro-sequence, the C-terminal pro-sequence or both pro-sequences, toward the pro-form with both N- and C-terminal pro-sequences. The data indicate that the pro-forms of the enzyme have proteolytic activity, and are stimulated by the same proteolytic activity. The stimulation occurs in two steps, with approximately eightfold stimulation by N-terminal cleavage, approximately fourfold stimulation by C-terminal cleavage, and 23-fold stimulation by the cleavage of both termini, compared to the pro-form with both the N- and C-terminal pro-sequences. Such cleavage mainly occurs in a trans manner; i.e. the pro-form dimer cleaves the monomeric form. The stimulation by N-terminal pro-sequence removal is due to the cis (intra-dimer and inter-protomer) effect of formation of the new N-terminus, whereas that by C-terminal cleavage is due to removal of its trans (inter-dimer) inhibitory effect. A numerical simulation of the maturation pathway is presented.</div>
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<affiliations><list><country><li>Japon</li>
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<tree><noCountry><name sortKey="Kim, Yong Tae" sort="Kim, Yong Tae" uniqKey="Kim Y" first="Yong-Tae" last="Kim">Yong-Tae Kim</name>
<name sortKey="Nishii, Wataru" sort="Nishii, Wataru" uniqKey="Nishii W" first="Wataru" last="Nishii">Wataru Nishii</name>
<name sortKey="Shirouzu, Mikako" sort="Shirouzu, Mikako" uniqKey="Shirouzu M" first="Mikako" last="Shirouzu">Mikako Shirouzu</name>
<name sortKey="Terada, Takaho" sort="Terada, Takaho" uniqKey="Terada T" first="Takaho" last="Terada">Takaho Terada</name>
<name sortKey="Yokoyama, Shigeyuki" sort="Yokoyama, Shigeyuki" uniqKey="Yokoyama S" first="Shigeyuki" last="Yokoyama">Shigeyuki Yokoyama</name>
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<country name="Japon"><noRegion><name sortKey="Muramatsu, Tomonari" sort="Muramatsu, Tomonari" uniqKey="Muramatsu T" first="Tomonari" last="Muramatsu">Tomonari Muramatsu</name>
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Autoprocessing mechanism of severe acute respiratory syndrome coronavirus 3C-like protease (SARS-CoV 3CLpro) from its polyproteins.

Autoprocessing mechanism of severe acute respiratory syndrome coronavirus 3C-like protease (SARS-CoV 3CLpro) from its polyproteins.

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