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 : 001616The 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 ValloneSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2006.
Descripteurs français
- KwdFr :
- Alignement de séquences, Animaux, Cristallographie aux rayons X, Données de séquences moléculaires, Endoribonucleases (), Endoribonucleases (génétique), Endoribonucleases (métabolisme), Humains, Maturation post-transcriptionnelle des ARN, Modèles moléculaires, Petit ARN nucléaire (métabolisme), Pliage des protéines, Protéines de Xénope (), Protéines de Xénope (génétique), Protéines de Xénope (métabolisme), Réplication virale (physiologie), Sites de fixation, Structure tertiaire des protéines, Séquence d'acides aminés, Uridine monophosphate (métabolisme), Virus du SRAS (génétique), Virus du SRAS (physiologie), Xenopus laevis (métabolisme).
- MESH :
- génétique : Endoribonucleases, Protéines de Xénope, Virus du SRAS.
- métabolisme : Endoribonucleases, Petit ARN nucléaire, Protéines de Xénope, Uridine monophosphate, Xenopus laevis.
- physiologie : Réplication virale, Virus du SRAS.
- Alignement de séquences, Animaux, Cristallographie aux rayons X, Données de séquences moléculaires, Endoribonucleases, Humains, Maturation post-transcriptionnelle des ARN, Modèles moléculaires, Pliage des protéines, Protéines de Xénope, Sites de fixation, Structure tertiaire des protéines, Séquence d'acides aminés.
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:16895992Le document en format XML
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<term>Maturation post-transcriptionnelle des ARN</term>
<term>Modèles moléculaires</term>
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<term>Protéines de Xénope</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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<Abstract><AbstractText>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.</AbstractText>
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<affiliations><list><country><li>Italie</li>
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