Hinweise zu Qualitätskriterien von Zeitschriften
Open-Access-Richtlinie der Helmholtz-Gemeinschaft 2016
CC Licencences
Metriken für Publikationen
Startseite
Login
English
Neuer EVA Antrag
Erweiterte Suche
Durchblättern nach ...
Publikationen im Überblick
HGF Fortschrittsbericht
OA Publikationen
Neue Publikation eintragen
Neue Publikation holen aus...
Fehlende Publikation melden
Ansprechpartner
Hilfe
Bibliometrische Indikatoren
Text
Endnote (RIS)
BibTeX
Verlagsversion
Forschungsdaten
DOI
PMC
 |
Open Access Gold |
|
möglich sobald bei der ZB eingereicht worden ist.
Modulation of HIV-1 gene expression by binding of a ULM motif in the Rev protein to UHM-containing splicing factors.
Nucleic Acids Res. 47, 4859-4871 (2019)
Verlagsversion
Forschungsdaten
DOI
PMC
The HIV-1 protein Rev is essential for virus replication and ensures the expression of partially spliced and unspliced transcripts. We identified a ULM (UHM ligand motif) motif in the Arginine-Rich Motif (ARM) of the Rev protein. ULMs (UHM ligand motif) mediate protein interactions during spliceosome assembly by binding to UHM (U2AF homology motifs) domains. Using NMR, biophysical methods and crystallography we show that the Rev ULM binds to the UHMs of U2AF65 and SPF45. The highly conserved Trp45 in the Rev ULM is crucial for UHM binding in vitro, for Rev co-precipitation with U2AF65 in human cells and for proper processing of HIV transcripts. Thus, Rev-ULM interactions with UHM splicing factors contribute to the regulation of HIV-1 transcript processing, also at the splicing level. The Rev ULM is an example of viral mimicry of host short linear motifs that enables the virus to interfere with the host molecular machinery.
Impact Factor
Scopus SNIP
Web of Science
Times Cited
Times Cited
Scopus
Cited By
Cited By
Altmetric
11.147
3.156
1
3
Anmerkungen
Besondere Publikation
Auf Hompepage verbergern
Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
U2af Homology Motif; Rna Recognition; Terminal Domain; In-vitro; Peptide; Translation; Expansion; Sf3b155; Design
Sprache
englisch
Veröffentlichungsjahr
2019
HGF-Berichtsjahr
2019
ISSN (print) / ISBN
0305-1048
e-ISSN
1362-4962
Zeitschrift
Nucleic Acids Research
Quellenangaben
Band: 47,
Heft: 9,
Seiten: 4859-4871
Verlag
Oxford University Press
Verlagsort
Great Clarendon St, Oxford Ox2 6dp, England
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Structural Biology (STB)
Institute of Virology (VIRO)
Research Unit Signaling and Translation (SAT)
Institute of Virology (VIRO)
Research Unit Signaling and Translation (SAT)
POF Topic(s)
30203 - Molecular Targets and Therapies
Forschungsfeld(er)
Enabling and Novel Technologies
Immune Response and Infection
Immune Response and Infection
PSP-Element(e)
G-503000-001
G-502700-009
G-502700-001
G-509800-002
G-502700-009
G-502700-001
G-509800-002
WOS ID
WOS:000473756300042
Scopus ID
85066058174
PubMed ID
30892606
Erfassungsdatum
2019-03-26