SrasV1, PubMed, Checkpoint, bibRecord, 001627

New nsp8 isoform suggests mechanism for tuning viral RNA synthesis.

Identifieur interne : 001627 ( PubMed/Checkpoint ); précédent : 001626; suivant : 001628

New nsp8 isoform suggests mechanism for tuning viral RNA synthesis.

Auteurs : Shuang Li [République populaire de Chine] ; Qi Zhao ; Yinjie Zhang ; Yang Zhang ; Mark Bartlam ; Xuemei Li ; Zihe Rao

Source :

Protein & cell [ 1674-8018 ] ; 2010.

RBID : pubmed:21203988

Descripteurs français

KwdFr :
- ARN viral (biosynthèse), Alignement de séquences, Cristallographie aux rayons X, DNA primase (), DNA primase (génétique), DNA primase (physiologie), Données de séquences moléculaires, Humains, Isoenzymes (), Isoenzymes (génétique), Isoenzymes (physiologie), Réplication virale, Structure secondaire des protéines, Syndrome respiratoire aigu sévère (virologie), Séquence d'acides aminés, Virus du SRAS (), Virus du SRAS (génétique), Virus du SRAS (physiologie).
MESH :
- biosynthèse : ARN viral.
- génétique : DNA primase, Isoenzymes, Virus du SRAS.
- physiologie : DNA primase, Isoenzymes, Virus du SRAS.
- virologie : Syndrome respiratoire aigu sévère.
- Alignement de séquences, Cristallographie aux rayons X, DNA primase, Données de séquences moléculaires, Humains, Isoenzymes, Réplication virale, Structure secondaire des protéines, Séquence d'acides aminés, Virus du SRAS.

English descriptors

KwdEn :
- Amino Acid Sequence, Crystallography, X-Ray, DNA Primase (chemistry), DNA Primase (genetics), DNA Primase (physiology), Humans, Isoenzymes (chemistry), Isoenzymes (genetics), Isoenzymes (physiology), Molecular Sequence Data, Protein Structure, Secondary, RNA, Viral (biosynthesis), SARS Virus (chemistry), SARS Virus (genetics), SARS Virus (physiology), Sequence Alignment, Severe Acute Respiratory Syndrome (virology), Virus Replication.
MESH :
- chemical , biosynthesis : RNA, Viral.
- chemical , chemistry : DNA Primase, Isoenzymes.
- chemical , genetics : DNA Primase, Isoenzymes.
- chemical , physiology : DNA Primase, Isoenzymes.
- chemistry : SARS Virus.
- genetics : SARS Virus.
- physiology : SARS Virus.
- virology : Severe Acute Respiratory Syndrome.
- Amino Acid Sequence, Crystallography, X-Ray, Humans, Molecular Sequence Data, Protein Structure, Secondary, Sequence Alignment, Virus Replication.

Abstract

During severe acute respiratory syndrome coronavirus (SARS-CoV) infection, the activity of the replication/transcription complexes (RTC) quickly peaks at 6 hours post infection (h.p.i) and then diminishes significantly in the late post-infection stages. This "down-up-down" regulation of RNA synthesis distinguishes different viral stages: primary translation, genome replication, and finally viron assembly. Regarding the nsp8 as the primase in RNA synthesis, we confirmed that the proteolysis product of the primase (nsp8) contains the globular domain (nsp8C), and indentified the resectioning site that is notably conserved in all the three groups of coronavirus. We subsequently crystallized the complex of SARS-CoV nsp8C and nsp7, and the 3-D structure of this domain revealed its capability to interfuse into the hexadecamer super-complex. This specific proteolysis may indicate one possible mechanism by which coronaviruses to switch from viral infection to genome replication and viral assembly stages.

DOI: 10.1007/s13238-010-0028-8
PubMed: 21203988

Affiliations:

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

to stream PubMed, to step Corpus: 001568
to stream PubMed, to step Curation: 001568

Links to Exploration step

pubmed:21203988

Le document en format XML

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<front><div type="abstract" xml:lang="en">During severe acute respiratory syndrome coronavirus (SARS-CoV) infection, the activity of the replication/transcription complexes (RTC) quickly peaks at 6 hours post infection (h.p.i) and then diminishes significantly in the late post-infection stages. This "down-up-down" regulation of RNA synthesis distinguishes different viral stages: primary translation, genome replication, and finally viron assembly. Regarding the nsp8 as the primase in RNA synthesis, we confirmed that the proteolysis product of the primase (nsp8) contains the globular domain (nsp8C), and indentified the resectioning site that is notably conserved in all the three groups of coronavirus. We subsequently crystallized the complex of SARS-CoV nsp8C and nsp7, and the 3-D structure of this domain revealed its capability to interfuse into the hexadecamer super-complex. This specific proteolysis may indicate one possible mechanism by which coronaviruses to switch from viral infection to genome replication and viral assembly stages.</div>
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EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/PubMed/Checkpoint

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001627 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd -nk 001627 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Sante
   |area=    SrasV1
   |flux=    PubMed
   |étape=   Checkpoint
   |type=    RBID
   |clé=     pubmed:21203988
   |texte=   New nsp8 isoform suggests mechanism for tuning viral RNA synthesis.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Checkpoint/RBID.i   -Sk "pubmed:21203988" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd   \
       | NlmPubMed2Wicri -a SrasV1

This area was generated with Dilib version V0.6.33.
Data generation: Tue Apr 28 14:49:16 2020. Site generation: Sat Mar 27 22:06:49 2021

	Serveur d'exploration SRAS
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Serveur d'exploration SRAS

New nsp8 isoform suggests mechanism for tuning viral RNA synthesis.

New nsp8 isoform suggests mechanism for tuning viral RNA synthesis.

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Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki