HIV-1 matrix-tRNA complex structure reveals basis for host control of Gag localization.

Binding Sites Cell Membrane / metabolism HEK293 Cells HIV Antigens / metabolism HIV-1 / genetics HeLa Cells Humans Protein Domains / physiology RNA, Transfer / genetics RNA-Binding Proteins / metabolism Virus Assembly / physiology gag Gene Products, Human Immunodeficiency Virus / metabolism
Gag HIV RNA-protein interactions assembly host-pathogen interactions localization matrix plasma membrane tRNA

Journal

Cell host & microbe
ISSN: 1934-6069
Titre abrégé: Cell Host Microbe
Pays: United States
ID NLM: 101302316

Informations de publication

Date de publication:
08 09 2021
Historique:
received: 18 02 2021
revised: 24 05 2021
accepted: 19 07 2021
pubmed: 14 8 2021
medline: 14 1 2022
entrez: 13 8 2021
Statut: ppublish

Résumé

The HIV-1 virion structural polyprotein, Gag, is directed to particle assembly sites at the plasma membrane by its N-terminal matrix (MA) domain. MA also binds to host tRNAs. To understand the molecular basis of MA-tRNA interaction and its potential function, we present a co-crystal structure of HIV-1 MA-tRNA

Identifiants

DOI: 10.1016/j.chom.2021.07.006 PMID: 34384537 PMC: PMC8650744
pubmed: 34384537
pii: S1931-3128(21)00339-5
doi: 10.1016/j.chom.2021.07.006
pmc: PMC8650744
mid: NIHMS1732739
pii:
doi:

Substances chimiques

HIV Antigens 0
RNA-Binding Proteins 0
gag Gene Products, Human Immunodeficiency Virus 0
p17 protein, Human Immunodeficiency Virus Type 1 0
RNA, Transfer 9014-25-9

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, N.I.H., Intramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1421-1436.e7

Subventions

Organisme : NIAID NIH HHS
ID : U54 AI150470
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI150498
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI050111
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI050470
Pays : United States
Organisme : Intramural NIH HHS
ID : ZIA DK075136
Pays : United States
Organisme : Intramural NIH HHS
ID : Z99 DK999999
Pays : United States
Organisme : Howard Hughes Medical Institute
Pays : United States

Informations de copyright

Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests The authors declare no competing interests.

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Auteurs

Charles Bou-Nader (C)

Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892, USA.

Frauke Muecksch (F)

Laboratory of Retrovirology, The Rockefeller University, New York, NY 10065, USA.

Janae B Brown (JB)

Department of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, MD 21250, USA.

Jackson M Gordon (JM)

Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892, USA.

Ashley York (A)

Laboratory of Retrovirology, The Rockefeller University, New York, NY 10065, USA.

Chen Peng (C)

Laboratory of Retrovirology, The Rockefeller University, New York, NY 10065, USA.

Rodolfo Ghirlando (R)

Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892, USA.

Michael F Summers (MF)

Department of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, MD 21250, USA; Howard Hughes Medical Institute, University of Maryland, Baltimore County, Baltimore, MD 21250, USA.

Paul D Bieniasz (PD)

Laboratory of Retrovirology, The Rockefeller University, New York, NY 10065, USA; Howard Hughes Medical Institute, The Rockefeller University, New York, NY 10065, USA. Electronic address: pbieniasz@rockefeller.edu.

Jinwei Zhang (J)

Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892, USA. Electronic address: jinwei.zhang@nih.gov.

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Classifications MeSH

questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Sites de fixation › HIV-1 matrix-tRNA complex structure reveals...
questionsmedicales.fr › Cellules › Structures cellulaires › Membrane cellulaire › HIV-1 matrix-tRNA complex structure reveals...
questionsmedicales.fr › Cellules › Cellules épithéliales › Cellules HEK293 › HIV-1 matrix-tRNA complex structure reveals...
questionsmedicales.fr › Facteurs biologiques › Antigènes › Antigènes viraux › Antigènes du VIH › HIV-1 matrix-tRNA complex structure reveals...
questionsmedicales.fr › Virus › Virus à ARN › Retroviridae › Lentivirus › Lentivirus des primates › VIH (Virus de l'Immunodéficience Humaine) › VIH-1 (Virus de l'Immunodéficience Humaine de type 1) › HIV-1 matrix-tRNA complex structure reveals...
questionsmedicales.fr › Cellules › Cellules épithéliales › Cellules HeLa › HIV-1 matrix-tRNA complex structure reveals...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › HIV-1 matrix-tRNA complex structure reveals...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Structure tertiaire des protéines › Domaines protéiques › HIV-1 matrix-tRNA complex structure reveals...
questionsmedicales.fr › Acides nucléiques, nucléotides et nucléosides › Acides nucléiques › ARN › ARN de transfert › HIV-1 matrix-tRNA complex structure reveals...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Nucléoprotéines › Protéines de liaison à l'ARN › HIV-1 matrix-tRNA complex structure reveals...
questionsmedicales.fr › Phénomènes microbiologiques › Phénomènes physiologiques viraux › Réplication virale › Assemblage viral › HIV-1 matrix-tRNA complex structure reveals...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines virales › Protéines virales structurales › Protéines nucléocapside › Protéines du core viral › Produits du gène gag › Produits du gène gag du virus de l'immunodéficience humaine › HIV-1 matrix-tRNA complex structure reveals...