Atomic structure of the translation regulatory protein NS1 of bluetongue virus.
Journal
Nature microbiology
ISSN: 2058-5276
Titre abrégé: Nat Microbiol
Pays: England
ID NLM: 101674869
Informations de publication
Date de publication:
05 2019
05 2019
Historique:
received:
16
10
2018
accepted:
11
01
2019
pubmed:
20
2
2019
medline:
27
6
2019
entrez:
20
2
2019
Statut:
ppublish
Résumé
Bluetongue virus (BTV) non-structural protein 1 (NS1) regulates viral protein synthesis and exists as tubular and non-tubular forms in infected cells, but how tubules assemble and how protein synthesis is regulated are unknown. Here, we report near-atomic resolution structures of two NS1 tubular forms determined by cryo-electron microscopy. The two tubular forms are different helical assemblies of the same NS1 monomer, consisting of an amino-terminal foot, a head and body domains connected to an extended carboxy-terminal arm, which wraps atop the head domain of another NS1 subunit through hydrophobic interactions. Deletion of the C terminus prevents tubule formation but not viral replication, suggesting an active non-tubular form. Two zinc-finger-like motifs are present in each NS1 monomer, and tubules are disrupted by divalent cation chelation and restored by cation addition, including Zn
Identifiants
pubmed: 30778144
doi: 10.1038/s41564-019-0369-x
pii: 10.1038/s41564-019-0369-x
pmc: PMC6482088
mid: NIHMS1518569
doi:
Substances chimiques
Viral Nonstructural Proteins
0
Zinc
J41CSQ7QDS
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
837-845Subventions
Organisme : Wellcome Trust
ID : 100218
Pays : United Kingdom
Organisme : NIAID NIH HHS
ID : R01 AI094386
Pays : United States
Organisme : NIH HHS
ID : S10 OD018111
Pays : United States
Organisme : NIGMS NIH HHS
ID : U24 GM116792
Pays : United States
Organisme : Wellcome Trust
Pays : United Kingdom
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