Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling
- Autores
- El Mekdad, Hala; Boutant, Emmanuel; Karnib, Hassan; Biedma, Marina Elizabeth; Sharma, Kamal Kant; Malytska, Iuliia; Laumond, Géraldine; Roy, Marion; Réal, Eléonore; Paillart, Jean Christophe; Moog, Christiane; Darlix, Jean Luc; Mély, Yves; de Rocquigny, Hugues
- Año de publicación
- 2016
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Background: In HIV-1 infected cells, the integrated viral DNA is transcribed by the host cell machinery to generate the full length HIV-1 RNA (FL RNA) that serves as mRNA encoding for the Gag and GagPol precursors. Virion formation is orchestrated by Gag, and the current view is that a specific interaction between newly made Gag molecules and FL RNA initiates the process. This in turn would cause FL RNA dimerization by the NC domain of Gag (GagNC). However the RNA chaperoning activity of unprocessed Gag is low as compared to the mature NC protein. This prompted us to search for GagNC co-factors. Results: Here we report that RPL7, a major ribosomal protein involved in translation regulation, is a partner of Gag via its interaction with the NC domain. This interaction is mediated by the NC zinc fingers and the N- and C-termini of RPL7, respectively, but seems independent of RNA binding, Gag oligomerization and its interaction with the plasma membrane. Interestingly, RPL7 is shown for the first time to exhibit a potent DNA/RNA chaperone activity higher than that of Gag. In addition, Gag and RPL7 can function in concert to drive rapid nucleic acid hybridization. Conclusions: Our results show that GagNC interacts with the ribosomal protein RPL7 endowed with nucleic acid chaperone activity, favoring the notion that RPL7 could be a Gag helper chaperoning factor possibly contributing to the start of Gag assembly.
Instituto de Estudios Inmunológicos y Fisiopatológicos - Materia
-
Biología
HIV
Gag
RPL7
Interaction
Chaperone activity
Nucleocapsid - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by/4.0/
- Repositorio
.jpg)
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/97566
Ver los metadatos del registro completo
| id |
SEDICI_2ae327c3eb6c91a2c85b8a243fe07286 |
|---|---|
| oai_identifier_str |
oai:sedici.unlp.edu.ar:10915/97566 |
| network_acronym_str |
SEDICI |
| repository_id_str |
1329 |
| network_name_str |
SEDICI (UNLP) |
| spelling |
Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodelingEl Mekdad, HalaBoutant, EmmanuelKarnib, HassanBiedma, Marina ElizabethSharma, Kamal KantMalytska, IuliiaLaumond, GéraldineRoy, MarionRéal, EléonorePaillart, Jean ChristopheMoog, ChristianeDarlix, Jean LucMély, Yvesde Rocquigny, HuguesBiologíaHIVGagRPL7InteractionChaperone activityNucleocapsidBackground: In HIV-1 infected cells, the integrated viral DNA is transcribed by the host cell machinery to generate the full length HIV-1 RNA (FL RNA) that serves as mRNA encoding for the Gag and GagPol precursors. Virion formation is orchestrated by Gag, and the current view is that a specific interaction between newly made Gag molecules and FL RNA initiates the process. This in turn would cause FL RNA dimerization by the NC domain of Gag (GagNC). However the RNA chaperoning activity of unprocessed Gag is low as compared to the mature NC protein. This prompted us to search for GagNC co-factors. Results: Here we report that RPL7, a major ribosomal protein involved in translation regulation, is a partner of Gag via its interaction with the NC domain. This interaction is mediated by the NC zinc fingers and the N- and C-termini of RPL7, respectively, but seems independent of RNA binding, Gag oligomerization and its interaction with the plasma membrane. Interestingly, RPL7 is shown for the first time to exhibit a potent DNA/RNA chaperone activity higher than that of Gag. In addition, Gag and RPL7 can function in concert to drive rapid nucleic acid hybridization. Conclusions: Our results show that GagNC interacts with the ribosomal protein RPL7 endowed with nucleic acid chaperone activity, favoring the notion that RPL7 could be a Gag helper chaperoning factor possibly contributing to the start of Gag assembly.Instituto de Estudios Inmunológicos y Fisiopatológicos2016-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf1-14http://sedici.unlp.edu.ar/handle/10915/97566enginfo:eu-repo/semantics/altIdentifier/url/https://ri.conicet.gov.ar/11336/57847info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4982112/info:eu-repo/semantics/altIdentifier/url/https://retrovirology.biomedcentral.com/articles/10.1186/s12977-016-0287-4info:eu-repo/semantics/altIdentifier/issn/1742-4690info:eu-repo/semantics/altIdentifier/doi/10.1186/s12977-016-0287-4info:eu-repo/semantics/altIdentifier/hdl/11336/57847info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-10-22T17:01:05Zoai:sedici.unlp.edu.ar:10915/97566Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-10-22 17:01:05.789SEDICI (UNLP) - Universidad Nacional de La Platafalse |
| dc.title.none.fl_str_mv |
Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling |
| title |
Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling |
| spellingShingle |
Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling El Mekdad, Hala Biología HIV Gag RPL7 Interaction Chaperone activity Nucleocapsid |
| title_short |
Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling |
| title_full |
Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling |
| title_fullStr |
Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling |
| title_full_unstemmed |
Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling |
| title_sort |
Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling |
| dc.creator.none.fl_str_mv |
El Mekdad, Hala Boutant, Emmanuel Karnib, Hassan Biedma, Marina Elizabeth Sharma, Kamal Kant Malytska, Iuliia Laumond, Géraldine Roy, Marion Réal, Eléonore Paillart, Jean Christophe Moog, Christiane Darlix, Jean Luc Mély, Yves de Rocquigny, Hugues |
| author |
El Mekdad, Hala |
| author_facet |
El Mekdad, Hala Boutant, Emmanuel Karnib, Hassan Biedma, Marina Elizabeth Sharma, Kamal Kant Malytska, Iuliia Laumond, Géraldine Roy, Marion Réal, Eléonore Paillart, Jean Christophe Moog, Christiane Darlix, Jean Luc Mély, Yves de Rocquigny, Hugues |
| author_role |
author |
| author2 |
Boutant, Emmanuel Karnib, Hassan Biedma, Marina Elizabeth Sharma, Kamal Kant Malytska, Iuliia Laumond, Géraldine Roy, Marion Réal, Eléonore Paillart, Jean Christophe Moog, Christiane Darlix, Jean Luc Mély, Yves de Rocquigny, Hugues |
| author2_role |
author author author author author author author author author author author author author |
| dc.subject.none.fl_str_mv |
Biología HIV Gag RPL7 Interaction Chaperone activity Nucleocapsid |
| topic |
Biología HIV Gag RPL7 Interaction Chaperone activity Nucleocapsid |
| dc.description.none.fl_txt_mv |
Background: In HIV-1 infected cells, the integrated viral DNA is transcribed by the host cell machinery to generate the full length HIV-1 RNA (FL RNA) that serves as mRNA encoding for the Gag and GagPol precursors. Virion formation is orchestrated by Gag, and the current view is that a specific interaction between newly made Gag molecules and FL RNA initiates the process. This in turn would cause FL RNA dimerization by the NC domain of Gag (GagNC). However the RNA chaperoning activity of unprocessed Gag is low as compared to the mature NC protein. This prompted us to search for GagNC co-factors. Results: Here we report that RPL7, a major ribosomal protein involved in translation regulation, is a partner of Gag via its interaction with the NC domain. This interaction is mediated by the NC zinc fingers and the N- and C-termini of RPL7, respectively, but seems independent of RNA binding, Gag oligomerization and its interaction with the plasma membrane. Interestingly, RPL7 is shown for the first time to exhibit a potent DNA/RNA chaperone activity higher than that of Gag. In addition, Gag and RPL7 can function in concert to drive rapid nucleic acid hybridization. Conclusions: Our results show that GagNC interacts with the ribosomal protein RPL7 endowed with nucleic acid chaperone activity, favoring the notion that RPL7 could be a Gag helper chaperoning factor possibly contributing to the start of Gag assembly. Instituto de Estudios Inmunológicos y Fisiopatológicos |
| description |
Background: In HIV-1 infected cells, the integrated viral DNA is transcribed by the host cell machinery to generate the full length HIV-1 RNA (FL RNA) that serves as mRNA encoding for the Gag and GagPol precursors. Virion formation is orchestrated by Gag, and the current view is that a specific interaction between newly made Gag molecules and FL RNA initiates the process. This in turn would cause FL RNA dimerization by the NC domain of Gag (GagNC). However the RNA chaperoning activity of unprocessed Gag is low as compared to the mature NC protein. This prompted us to search for GagNC co-factors. Results: Here we report that RPL7, a major ribosomal protein involved in translation regulation, is a partner of Gag via its interaction with the NC domain. This interaction is mediated by the NC zinc fingers and the N- and C-termini of RPL7, respectively, but seems independent of RNA binding, Gag oligomerization and its interaction with the plasma membrane. Interestingly, RPL7 is shown for the first time to exhibit a potent DNA/RNA chaperone activity higher than that of Gag. In addition, Gag and RPL7 can function in concert to drive rapid nucleic acid hybridization. Conclusions: Our results show that GagNC interacts with the ribosomal protein RPL7 endowed with nucleic acid chaperone activity, favoring the notion that RPL7 could be a Gag helper chaperoning factor possibly contributing to the start of Gag assembly. |
| publishDate |
2016 |
| dc.date.none.fl_str_mv |
2016-07 |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Articulo http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
| format |
article |
| status_str |
publishedVersion |
| dc.identifier.none.fl_str_mv |
http://sedici.unlp.edu.ar/handle/10915/97566 |
| url |
http://sedici.unlp.edu.ar/handle/10915/97566 |
| dc.language.none.fl_str_mv |
eng |
| language |
eng |
| dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://ri.conicet.gov.ar/11336/57847 info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4982112/ info:eu-repo/semantics/altIdentifier/url/https://retrovirology.biomedcentral.com/articles/10.1186/s12977-016-0287-4 info:eu-repo/semantics/altIdentifier/issn/1742-4690 info:eu-repo/semantics/altIdentifier/doi/10.1186/s12977-016-0287-4 info:eu-repo/semantics/altIdentifier/hdl/11336/57847 |
| dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) |
| eu_rights_str_mv |
openAccess |
| rights_invalid_str_mv |
http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) |
| dc.format.none.fl_str_mv |
application/pdf 1-14 |
| dc.source.none.fl_str_mv |
reponame:SEDICI (UNLP) instname:Universidad Nacional de La Plata instacron:UNLP |
| reponame_str |
SEDICI (UNLP) |
| collection |
SEDICI (UNLP) |
| instname_str |
Universidad Nacional de La Plata |
| instacron_str |
UNLP |
| institution |
UNLP |
| repository.name.fl_str_mv |
SEDICI (UNLP) - Universidad Nacional de La Plata |
| repository.mail.fl_str_mv |
alira@sedici.unlp.edu.ar |
| _version_ |
1846783257296764928 |
| score |
12.982451 |