Modulation of HIV-1 gene expression by binding of a ULM motif
in the Rev protein to UHM-containing splicing factors

J 2019

Modulation of HIV-1 gene expression by binding of a ULM motif in the Rev protein to UHM-containing splicing factors

PABIS, M., L. CORSINI, M. VINCENDEAU, Konstantinos TRIPSIANES, T.J. GIBSON et. al.

Základní údaje

Originální název

Modulation of HIV-1 gene expression by binding of a ULM motif in the Rev protein to UHM-containing splicing factors

Autoři

PABIS, M. (276 Německo), L. CORSINI (276 Německo), M. VINCENDEAU (276 Německo), Konstantinos TRIPSIANES (300 Řecko, garant, domácí), T.J. GIBSON (276 Německo), R. BRACK-WERNER (276 Německo) a M. SATTLER (276 Německo)

Vydání

Nucleic acids research, Oxford, Oxford University Press, 2019, 0305-1048

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 11.502

Kód RIV

RIV/00216224:14740/19:00110454

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1093/nar/gkz185

UT WoS

000473756300042

Klíčová slova anglicky

U2AF HOMOLOGY MOTIF; RNA RECOGNITION; TERMINAL DOMAIN; IN-VITRO; PEPTIDE; TRANSLATION; EXPANSION; SF3B155; DESIGN

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 4. 3. 2020 13:28, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

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.

Návaznosti

LQ1601, projekt VaV

Název: CEITEC 2020 (Akronym: CEITEC2020)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CEITEC 2020

Citovat

PABIS, M., L. CORSINI, M. VINCENDEAU, Konstantinos TRIPSIANES, T.J. GIBSON, R. BRACK-WERNER a M. SATTLER. Modulation of HIV-1 gene expression by binding of a ULM motif in the Rev protein to UHM-containing splicing factors. Nucleic acids research. Oxford: Oxford University Press, 2019, roč. 47, č. 9, s. 4859-4871. ISSN 0305-1048. Dostupné z: https://dx.doi.org/10.1093/nar/gkz185.

@article{1549793,
   author = {Pabis, M. and Corsini, L. and Vincendeau, M. and Tripsianes, Konstantinos and Gibson, T.J. and BrackandWerner, R. and Sattler, M.},
   article_location = {Oxford},
   article_number = {9},
   doi = {http://dx.doi.org/10.1093/nar/gkz185},
   keywords = {U2AF HOMOLOGY MOTIF; RNA RECOGNITION; TERMINAL DOMAIN; IN-VITRO; PEPTIDE; TRANSLATION; EXPANSION; SF3B155; DESIGN},
   language = {eng},
   issn = {0305-1048},
   journal = {Nucleic acids research},
   title = {Modulation of HIV-1 gene expression by binding of a ULM motif in the Rev protein to UHM-containing splicing factors},
   url = {https://watermark.silverchair.com/gkz185.pdf?token=AQECAHi208BE49Ooan9kkhW_Ercy7Dm3ZL_9Cf3qfKAc485ysgAAAk8wggJLBgkqhkiG9w0BBwagggI8MIICOAIBADCCAjEGCSqGSIb3DQEHATAeBglghkgBZQMEAS4wEQQMZzyNa5PwEnDOIB7CAgEQgIICAmJux6ctUXEbbjGsyOkoACJ-XChVYwyJ6xBNvib1iKntadf},
   volume = {47},
   year = {2019}
}

TY  - JOUR
ID  - 1549793
AU  - Pabis, M. - Corsini, L. - Vincendeau, M. - Tripsianes, Konstantinos - Gibson, T.J. - Brack-Werner, R. - Sattler, M.
PY  - 2019
TI  - Modulation of HIV-1 gene expression by binding of a ULM motif in the Rev protein to UHM-containing splicing factors
JF  - Nucleic acids research
VL  - 47
IS  - 9
SP  - 4859-4871
EP  - 4859-4871
PB  - Oxford University Press
SN  - 03051048
KW  - U2AF HOMOLOGY MOTIF
KW  - RNA RECOGNITION
KW  - TERMINAL DOMAIN
KW  - IN-VITRO
KW  - PEPTIDE
KW  - TRANSLATION
KW  - EXPANSION
KW  - SF3B155
KW  - DESIGN
UR  - https://watermark.silverchair.com/gkz185.pdf?token=AQECAHi208BE49Ooan9kkhW_Ercy7Dm3ZL_9Cf3qfKAc485ysgAAAk8wggJLBgkqhkiG9w0BBwagggI8MIICOAIBADCCAjEGCSqGSIb3DQEHATAeBglghkgBZQMEAS4wEQQMZzyNa5PwEnDOIB7CAgEQgIICAmJux6ctUXEbbjGsyOkoACJ-XChVYwyJ6xBNvib1iKntadf
L2  - https://watermark.silverchair.com/gkz185.pdf?token=AQECAHi208BE49Ooan9kkhW_Ercy7Dm3ZL_9Cf3qfKAc485ysgAAAk8wggJLBgkqhkiG9w0BBwagggI8MIICOAIBADCCAjEGCSqGSIb3DQEHATAeBglghkgBZQMEAS4wEQQMZzyNa5PwEnDOIB7CAgEQgIICAmJux6ctUXEbbjGsyOkoACJ-XChVYwyJ6xBNvib1iKntadf
N2  - 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.
ER  -

PABIS, M., L. CORSINI, M. VINCENDEAU, Konstantinos TRIPSIANES, T.J. GIBSON, R. BRACK-WERNER a M. SATTLER. Modulation of HIV-1 gene expression by binding of a ULM motif in the Rev protein to UHM-containing splicing factors. \textit{Nucleic acids research}. Oxford: Oxford University Press, 2019, roč.~47, č.~9, s.~4859-4871. ISSN~0305-1048. Dostupné z: https://dx.doi.org/10.1093/nar/gkz185.

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