SrasV1, Ncbi, Merge, bibRecord, 001615

The structure of the endoribonuclease XendoU: From small nucleolar RNA processing to severe acute respiratory syndrome coronavirus replication.

Identifieur interne : 001615 ( Ncbi/Merge ); précédent : 001614; suivant : 001616

The structure of the endoribonuclease XendoU: From small nucleolar RNA processing to severe acute respiratory syndrome coronavirus replication.

Auteurs : Fabiana Renzi [Italie] ; Elisa Caffarelli ; Pietro Laneve ; Irene Bozzoni ; Maurizio Brunori ; Beatrice Vallone

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2006.

RBID : pubmed:16895992

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Animals, Binding Sites, Crystallography, X-Ray, Endoribonucleases (chemistry), Endoribonucleases (genetics), Endoribonucleases (metabolism), Humans, Models, Molecular, Molecular Sequence Data, Protein Folding, Protein Structure, Tertiary, RNA Processing, Post-Transcriptional, RNA, Small Nuclear (metabolism), SARS Virus (genetics), SARS Virus (physiology), Sequence Alignment, Uridine Monophosphate (metabolism), Virus Replication (physiology), Xenopus Proteins (chemistry), Xenopus Proteins (genetics), Xenopus Proteins (metabolism), Xenopus laevis (metabolism).
MESH :
- chemical , chemistry : Endoribonucleases, Xenopus Proteins.
- chemical , genetics : Endoribonucleases, Xenopus Proteins.
- chemical , metabolism : Endoribonucleases, RNA, Small Nuclear, Uridine Monophosphate, Xenopus Proteins.
- genetics : SARS Virus.
- metabolism : Xenopus laevis.
- physiology : SARS Virus, Virus Replication.
- Amino Acid Sequence, Animals, Binding Sites, Crystallography, X-Ray, Humans, Models, Molecular, Molecular Sequence Data, Protein Folding, Protein Structure, Tertiary, RNA Processing, Post-Transcriptional, Sequence Alignment.

Abstract

Small nucleolar RNAs (snoRNAs) play a key role in eukaryotic ribosome biogenesis. In most cases, snoRNAs are encoded in introns and are released through the splicing reaction. Some snoRNAs are, instead, produced by an alternative pathway consisting of endonucleolytic processing of pre-mRNA. XendoU, the endoribonuclease responsible for this activity, is a U-specific, metal-dependent enzyme that releases products with 2'-3' cyclic phosphate termini. XendoU is broadly conserved among eukaryotes, and it is a genetic marker of nidoviruses, including the severe acute respiratory syndrome coronavirus, where it is essential for replication and transcription. We have determined by crystallography the structure of XendoU that, by refined search methodologies, appears to display a unique fold. Based on sequence conservation, mutagenesis, and docking simulations, we have identified the active site. The conserved structural determinants of this site may provide a framework for attempting to design antiviral drugs to interfere with the infectious nidovirus life cycle.

DOI: 10.1073/pnas.0602426103
PubMed: 16895992

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

to stream PubMed, to step Corpus: 002131
to stream PubMed, to step Curation: 002131
to stream PubMed, to step Checkpoint: 001F45

Links to Exploration step

pubmed:16895992

Le document en format XML

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<term>Endoribonucleases (genetics)</term>
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<front><div type="abstract" xml:lang="en">Small nucleolar RNAs (snoRNAs) play a key role in eukaryotic ribosome biogenesis. In most cases, snoRNAs are encoded in introns and are released through the splicing reaction. Some snoRNAs are, instead, produced by an alternative pathway consisting of endonucleolytic processing of pre-mRNA. XendoU, the endoribonuclease responsible for this activity, is a U-specific, metal-dependent enzyme that releases products with 2'-3' cyclic phosphate termini. XendoU is broadly conserved among eukaryotes, and it is a genetic marker of nidoviruses, including the severe acute respiratory syndrome coronavirus, where it is essential for replication and transcription. We have determined by crystallography the structure of XendoU that, by refined search methodologies, appears to display a unique fold. Based on sequence conservation, mutagenesis, and docking simulations, we have identified the active site. The conserved structural determinants of this site may provide a framework for attempting to design antiviral drugs to interfere with the infectious nidovirus life cycle.</div>
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<affiliations><list><country><li>Italie</li>
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<region><li>Latium</li>
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<settlement><li>Rome</li>
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<tree><noCountry><name sortKey="Bozzoni, Irene" sort="Bozzoni, Irene" uniqKey="Bozzoni I" first="Irene" last="Bozzoni">Irene Bozzoni</name>
<name sortKey="Brunori, Maurizio" sort="Brunori, Maurizio" uniqKey="Brunori M" first="Maurizio" last="Brunori">Maurizio Brunori</name>
<name sortKey="Caffarelli, Elisa" sort="Caffarelli, Elisa" uniqKey="Caffarelli E" first="Elisa" last="Caffarelli">Elisa Caffarelli</name>
<name sortKey="Laneve, Pietro" sort="Laneve, Pietro" uniqKey="Laneve P" first="Pietro" last="Laneve">Pietro Laneve</name>
<name sortKey="Vallone, Beatrice" sort="Vallone, Beatrice" uniqKey="Vallone B" first="Beatrice" last="Vallone">Beatrice Vallone</name>
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<country name="Italie"><region name="Latium"><name sortKey="Renzi, Fabiana" sort="Renzi, Fabiana" uniqKey="Renzi F" first="Fabiana" last="Renzi">Fabiana Renzi</name>
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The structure of the endoribonuclease XendoU: From small nucleolar RNA processing to severe acute respiratory syndrome coronavirus replication.

The structure of the endoribonuclease XendoU: From small nucleolar RNA processing to severe acute respiratory syndrome coronavirus replication.

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